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Conserved domains on  [gi|1741209931|ref|WP_149602109|]
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N-acetylmuramate alpha-1-phosphate uridylyltransferase MurU [Pseudoalteromonas distincta]

Protein Classification

nucleotidyltransferase family protein( domain architecture ID 11440233)

nucleotidyltransferase family protein such as Pseudomonas aeruginosa N-acetylmuramate alpha-1-phosphate uridylyltransferase MurU that catalyzes the formation of UDP-N-acetylmuramate (UDP-MurNAc), a crucial precursor of the bacterial peptidoglycan cell wall, from UTP and MurNAc-alpha-1P

EC:  2.7.7.-
Gene Ontology:  GO:0016779|GO:0009252
PubMed:  9445404
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-218 9.15e-79

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: 235.82  E-value: 9.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILYSQEvE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDE-G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931  82 GGLETAGGIIEALPLLGDS-FIVINGDVYTDYDVSVLMQLHLQPG-EAHIVLIENPPHNPDGDFALSHL----------S 149
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGaDATLALVPVPDPSRYGVVELDGDgrvtrfvekpE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931 150 AESQKYTFSGIGRYQADFFKGLTQGIR-PLGPILREKLNEHLVSTELYIGQWDDIGTPERLNQLNTRLEA 218
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPEGEPfDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-218 9.15e-79

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: 235.82  E-value: 9.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILYSQEvE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDE-G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931  82 GGLETAGGIIEALPLLGDS-FIVINGDVYTDYDVSVLMQLHLQPG-EAHIVLIENPPHNPDGDFALSHL----------S 149
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGaDATLALVPVPDPSRYGVVELDGDgrvtrfvekpE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931 150 AESQKYTFSGIGRYQADFFKGLTQGIR-PLGPILREKLNEHLVSTELYIGQWDDIGTPERLNQLNTRLEA 218
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPEGEPfDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-212 1.45e-77

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: 232.08  E-value: 1.45e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDgSQFGVNILYSQEVE 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931  82 GGLETAGGIIEALPLLG-DSFIVINGDVYTDYDVSVLMQLHL---QPGEAHIVLIENPPHNPDGDFALSH-------LSA 150
Cdd:cd06422    80 ELLETGGGIKKALPLLGdEPFLVVNGDILWDGDLAPLLLLHAwrmDALLLLLPLVRNPGHNGVGDFSLDAdgrlrrgGGG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1741209931 151 ESQKYTFSGIGRYQADFFKGLTQGIRPLGPILREKLNEHLVSTELYIGQWDDIGTPERLNQL 212
Cdd:cd06422   160 AVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-113 2.85e-39

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: 138.88  E-value: 2.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILYSQEV 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1741209931  81 EgGLETAGGIIEALPLLGDSFIVINGDVYTDYD 113
Cdd:TIGR03992  81 E-QLGTADALGSAKEYVDDEFLVLNGDVLLDSD 112
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-209 1.08e-28

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: 107.72  E-value: 1.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGK-PLIEHHINNLKAADITD-IVINLAWQGDKIKDYFKDGSQFGVNILYSQE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931  80 VEgGLETAGGIIEALPLLGDS---FIVINGDVYTDYDVSVLMQLHLQPGEAHIVLIENPPHNP---------DGDFALSH 147
Cdd:pfam00483  81 PE-GKGTAPAVALAADFLGDEksdVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPptgygvvefDDNGRVIR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1741209931 148 LS-----------AESQKYTF-SGIGRYQADFFKGLTQGIRPLGPILREKLNEHLVSTElYIG---QWDDIGTPERL 209
Cdd:pfam00483 160 FVekpklpkasnyASMGIYIFnSGVLDFLAKYLEELKRGEDEITDILPKALEDGKLAYA-FIFkgyAWLDVGTWDSL 235
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-135 4.72e-12

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 64.08  E-value: 4.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVnilysQEVEg 82
Cdd:PRK14354    5 AIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFAL-----QEEQ- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1741209931  83 gLETAGGIIEALPLLGDS---FIVINGDV--YTDYDVSVLMQLHLQPGEAHIVL---IENP 135
Cdd:PRK14354   76 -LGTGHAVMQAEEFLADKegtTLVICGDTplITAETLKNLIDFHEEHKAAATILtaiAENP 135
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-218 9.15e-79

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: 235.82  E-value: 9.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILYSQEvE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDE-G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931  82 GGLETAGGIIEALPLLGDS-FIVINGDVYTDYDVSVLMQLHLQPG-EAHIVLIENPPHNPDGDFALSHL----------S 149
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGaDATLALVPVPDPSRYGVVELDGDgrvtrfvekpE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931 150 AESQKYTFSGIGRYQADFFKGLTQGIR-PLGPILREKLNEHLVSTELYIGQWDDIGTPERLNQLNTRLEA 218
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPEGEPfDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-212 1.45e-77

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: 232.08  E-value: 1.45e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDgSQFGVNILYSQEVE 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931  82 GGLETAGGIIEALPLLG-DSFIVINGDVYTDYDVSVLMQLHL---QPGEAHIVLIENPPHNPDGDFALSH-------LSA 150
Cdd:cd06422    80 ELLETGGGIKKALPLLGdEPFLVVNGDILWDGDLAPLLLLHAwrmDALLLLLPLVRNPGHNGVGDFSLDAdgrlrrgGGG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1741209931 151 ESQKYTFSGIGRYQADFFKGLTQGIRPLGPILREKLNEHLVSTELYIGQWDDIGTPERLNQL 212
Cdd:cd06422   160 AVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-137 6.98e-46

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: 151.19  E-value: 6.98e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILYSQEVEg 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEE- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1741209931  83 GLETAGGIIEALPLLGDS-FIVINGDVYTDYDVSVLMQLHLQPGEAHIVLIENPPH 137
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDdFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVED 135
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-113 2.85e-39

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: 138.88  E-value: 2.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILYSQEV 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1741209931  81 EgGLETAGGIIEALPLLGDSFIVINGDVYTDYD 113
Cdd:TIGR03992  81 E-QLGTADALGSAKEYVDDEFLVLNGDVLLDSD 112
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-135 8.01e-36

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: 125.74  E-value: 8.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILYSQEVEg 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPE- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1741209931  83 GLETAGGIIEALPLL-GDSFIVINGDVYTDYDVSVLMQLHLQPG-EAHIVLIENP 135
Cdd:cd06915    80 PLGTGGAIKNALPKLpEDQFLVLNGDTYFDVDLLALLAALRASGaDATMALRRVP 134
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-123 4.20e-35

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: 123.78  E-value: 4.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILYSQEvEG 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVRE-DK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1741209931  83 GLETAGGIIEALPLLGDSFIVINGDVYTDYDVSVLMQLHLQ 123
Cdd:cd06426    80 PLGTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKE 120
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-135 4.85e-32

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: 116.13  E-value: 4.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILY-SQE 79
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYiLQE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931  80 VEGGLetAGGIIEALPLLGDS-FIVINGDVYTDYDVSVLMQLHLQPG-EAHIVL--IENP 135
Cdd:cd04189    81 EPLGL--AHAVLAARDFLGDEpFVVYLGDNLIQEGISPLVRDFLEEDaDASILLaeVEDP 138
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-144 8.45e-31

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: 112.71  E-value: 8.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDgsQFGVNILYSQEveg 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK--YPNIKFVYNPD--- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1741209931  83 gLETAGGIIE---ALPLLGDSFIVINGDVYtdYDVSVLMQLHLQPGEAHIVLieNPPHNPDGDFA 144
Cdd:cd02523    76 -YAETNNIYSlylARDFLDEDFLLLEGDVV--FDPSILERLLSSPADNAILV--DKKTKEWEDEY 135
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-120 2.74e-29

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 109.18  E-value: 2.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGS---QFGVNILYSQ 78
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGpdvTFVYNPDYDE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1741209931  79 EvegglETAGGIIEALPLLGDSFIVINGDVYtdYDVSVLMQL 120
Cdd:COG1213    81 T-----NNIYSLWLAREALDEDFLLLNGDVV--FDPAILKRL 115
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-209 1.08e-28

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: 107.72  E-value: 1.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGK-PLIEHHINNLKAADITD-IVINLAWQGDKIKDYFKDGSQFGVNILYSQE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931  80 VEgGLETAGGIIEALPLLGDS---FIVINGDVYTDYDVSVLMQLHLQPGEAHIVLIENPPHNP---------DGDFALSH 147
Cdd:pfam00483  81 PE-GKGTAPAVALAADFLGDEksdVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPptgygvvefDDNGRVIR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1741209931 148 LS-----------AESQKYTF-SGIGRYQADFFKGLTQGIRPLGPILREKLNEHLVSTElYIG---QWDDIGTPERL 209
Cdd:pfam00483 160 FVekpklpkasnyASMGIYIFnSGVLDFLAKYLEELKRGEDEITDILPKALEDGKLAYA-FIFkgyAWLDVGTWDSL 235
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-135 1.85e-25

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: 98.82  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQ-FGVNILYSQE 79
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKkLGIKITFSIE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1741209931  80 VEgGLETAGGIIEALPLLGDS---FIVINGDVYTDYDVSVLMQLHLQPG-EAHIVL--IENP 135
Cdd:cd06425    81 TE-PLGTAGPLALARDLLGDDdepFFVLNSDVICDFPLAELLDFHKKHGaEGTILVtkVEDP 141
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-107 2.65e-23

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 94.39  E-value: 2.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQ-GDKIKDYFKDGSQFGVNILY-SQ 78
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEdGPQFERLLGDGSQLGIKISYaVQ 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1741209931  79 EVEGGLetAGGIIEALPLLG-DSFIVINGD 107
Cdd:COG1209    81 PEPLGL--AHAFIIAEDFIGgDPVALVLGD 108
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-109 1.27e-18

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 80.64  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIkDYFKDgsQFGVNILYSQEv 80
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQF-EYLED--KYGVKLIYNPD- 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1741209931  81 eggLETAGGI---IEALPLLGDSFIvINGDVY 109
Cdd:COG4750    77 ---YAEYNNIsslYLVRDKLGNTYI-CSSDNY 104
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-131 1.75e-18

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: 81.15  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAG--RGQRMMPLTQNMPKPMLKVAGKPLIEHHINNL-KAADITDIVINLAWQGDKIKDYFKDGSQ-FGVNILYSQ 78
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQeFNVPIRYLQ 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931  79 EvEGGLETAGG-------IIEALPllgDSFIVINGDVYTDYDVSVLMQLHLQPGEAHIVL 131
Cdd:cd06428    81 E-YKPLGTAGGlyhfrdqILAGNP---SAFFVLNADVCCDFPLQELLEFHKKHGASGTIL 136
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-120 1.76e-18

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 79.99  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVNILYSQEV 80
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIVDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1741209931  81 EGGLE-----TAGGIIEALPLLGDSFIVINGDVYTDYDVSVLMQL 120
Cdd:cd02507    81 ITSDLcesagDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLEE 125
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-121 1.23e-17

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 77.70  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINL-----AWQGDKIKDYFKDGSQFGVNIL 75
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVpeeeqAEISTYLRSFPLNLKQKLDEVT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1741209931  76 YSQEVEGGleTAGGIIEALPLLGDSFIVINGDVYTDYDVSVLMQLH 121
Cdd:cd04198    81 IVLDEDMG--TADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLH 124
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-119 3.27e-16

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: 74.53  E-value: 3.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDI-VINLAWQGDKIKDYFKDGSQFGVNILYS-Q 78
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDLPLFKELLGDGSDLGIRITYAvQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1741209931  79 EVEGGLETAGGIIEALpLLGDSFIVINGD-VYTDYDVSVLMQ 119
Cdd:cd02538    81 PKPGGLAQAFIIGEEF-IGDDPVCLILGDnIFYGQGLSPILQ 121
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-120 8.42e-14

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: 68.33  E-value: 8.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYF-----------KDGSQ 69
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFdrsyeleetleKKGKT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1741209931  70 ----------FGVNILY-SQEVEGGLETAggIIEALPLLGD-SFIVINGDVYTDYDVSVLMQL 120
Cdd:cd02541    81 dlleevriisDLANIHYvRQKEPLGLGHA--VLCAKPFIGDePFAVLLGDDLIDSKEPCLKQL 141
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-108 5.99e-13

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: 66.97  E-value: 5.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDgsqFGVNILYSQEV 80
Cdd:COG1207     3 LAVVILAAGKGTRM---KSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD---LDVEFVLQEEQ 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1741209931  81 EGgleTAGGIIEALPLLGD---SFIVINGDV 108
Cdd:COG1207    77 LG---TGHAVQQALPALPGddgTVLVLYGDV 104
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-108 1.37e-12

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: 64.46  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDgsqFGVNILYSQEVEG 82
Cdd:cd02540     1 AVILAAGKGTRM---KSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALAN---PNVEFVLQEEQLG 74

                          90       100
                  ....*....|....*....|....*....
gi 1741209931  83 gleTAGGIIEALPLLGDS---FIVINGDV 108
Cdd:cd02540    75 ---TGHAVKQALPALKDFegdVLVLYGDV 100
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-107 3.47e-12

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 62.87  E-value: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmpltqNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDgsqFGVNILYSQEVEG 82
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAG---LGVRVVVNPDWEE 77

                          90       100
                  ....*....|....*....|....*...
gi 1741209931  83 GLET---AGgiIEALPLLGDSFIVINGD 107
Cdd:COG2068    78 GMSSslrAG--LAALPADADAVLVLLGD 103
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-135 4.72e-12

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 64.08  E-value: 4.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQFGVnilysQEVEg 82
Cdd:PRK14354    5 AIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFAL-----QEEQ- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1741209931  83 gLETAGGIIEALPLLGDS---FIVINGDV--YTDYDVSVLMQLHLQPGEAHIVL---IENP 135
Cdd:PRK14354   76 -LGTGHAVMQAEEFLADKegtTLVICGDTplITAETLKNLIDFHEEHKAAATILtaiAENP 135
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-107 9.33e-11

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: 58.73  E-value: 9.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmpltqNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGsqfGVNILYSQEVEG 82
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGL---PVVVVINPDWEE 74

                          90       100
                  ....*....|....*....|....*...
gi 1741209931  83 GLET---AGgiIEALPLLGDSFIVINGD 107
Cdd:cd04182    75 GMSSslaAG--LEALPADADAVLILLAD 100
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-123 1.64e-10

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: 58.39  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKD-------GSQFGVNIL 75
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKskwskpkSSLMIVIII 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1741209931  76 YSQEVegglETAGgiiEALPLL-------GDsFIVINGDVYTDYDVSVLMQLHLQ 123
Cdd:cd04197    83 MSEDC----RSLG---DALRDLdakglirGD-FILVSGDVVSNIDLKEILEEHKE 129
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-121 2.05e-10

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: 58.74  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKD----GSQFGVN----- 73
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNyflhNSDVTIDlgtnr 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1741209931  74 -ILYSQE--------VEGGLETA-GGIIEAL-PLLGD--SFIVINGDVYTDYDVSVLMQLH 121
Cdd:cd02524    81 iELHNSDiedwkvtlVDTGLNTMtGGRLKRVrRYLGDdeTFMLTYGDGVSDVNINALIEFH 141
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-119 1.58e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 56.61  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDI-VINLAWQGDKIKDYFKDGSQFGVNILYS-QE 79
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKvQP 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1741209931  80 VEGGLETAGGIIEALPLLGDSFIVINGDVYTDYDVSVLMQ 119
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLME 124
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-108 2.21e-09

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 54.12  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmpltqNMPKPMLKVAGKPLIEHHINNLKAAdITDIVINLAWqgDKIKDYFKDgsqFGVNILYSQEVEG 82
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPA-GDEVVVVAND--EEVLAALAG---LGVPVVPDPDPGQ 69

                          90       100
                  ....*....|....*....|....*...
gi 1741209931  83 GleTAGGIIEALPLLGDS--FIVINGDV 108
Cdd:pfam12804  70 G--PLAGLLAALRAAPGAdaVLVLACDM 95
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-51 2.58e-09

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 55.81  E-value: 2.58e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVI 51
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIF 54
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-104 7.22e-09

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: 53.68  E-value: 7.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNL-KAADITDIVINLAwqgDKIKDYFKDGSQFGVNILYSQeVE 81
Cdd:cd02516     3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFlAHPAIDEIVVVVP---PDDIDLAKELAKYGLSKVVKI-VE 75

                          90       100
                  ....*....|....*....|....*.
gi 1741209931  82 GGLETAGGI---IEALPLLGDSFIVI 104
Cdd:cd02516    76 GGATRQDSVlngLKALPDADPDIVLI 101
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-64 7.32e-09

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 54.53  E-value: 7.32e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1741209931   2 KAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYF 64
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHF 72
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-51 1.31e-08

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 53.21  E-value: 1.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1741209931   5 ILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNL-KAADITDIVI 51
Cdd:COG1211     2 IPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFlAHPRIDEIVV 46
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-111 2.90e-08

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 52.58  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQF---------- 70
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELeslleqrvkr 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1741209931  71 ------------GVNILYSQEVEgGLETAGGIIEALPLLGDS-FIVINGDVYTD 111
Cdd:PRK10122   84 qllaevqsicppGVTIMNVRQGQ-PLGLGHSILCARPAIGDNpFVVVLPDVVID 136
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-138 5.48e-08

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: 51.49  E-value: 5.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   5 ILAAGRGQRMMPLTQNMPKPMLKVAGKPLIEHHINNLKAadITDIVINLAWQGDKIKDYF-----KDGSQFGVNILYSQE 79
Cdd:cd04183     3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAK--IFDSRFIFICRDEHNTKFHldeslKLLAPNATVVELDGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1741209931  80 VEGGLETAGGIIEALPLLgDSFIVINGDVYTDYDVSVLMQLHLQPGEAHIVLIENPPHN 138
Cdd:cd04183    81 TLGAACTVLLAADLIDND-DPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP 138
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-109 2.31e-07

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 49.12  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   6 LAAGRGQRMmpltqNMP-KPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGsqfGVNIlysqeveggL 84
Cdd:COG2266     1 MAGGKGTRL-----GGGeKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKER---GVEV---------I 63

                          90       100       110
                  ....*....|....*....|....*....|
gi 1741209931  85 ETAGG-----IIEALPLLGDSFIVINGDVY 109
Cdd:COG2266    64 ETPGEgyvedLNEALESISGPVLVVPADLP 93
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-107 3.38e-07

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 49.99  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   5 ILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINnlKAADIT-DIVINLAWQGDKIKD----YFKdgsqfGVNIlYSQE 79
Cdd:PRK14359    7 ILAAGKGTRM---KSSLPKVLHTICGKPMLFYILK--EAFAISdDVHVVLHHQKERIKEavleYFP-----GVIF-HTQD 75

                          90       100
                  ....*....|....*....|....*...
gi 1741209931  80 VEGGLETaGGIIEALPLLGDSFIVINGD 107
Cdd:PRK14359   76 LENYPGT-GGALMGIEPKHERVLILNGD 102
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-104 4.38e-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: 48.34  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMmpltqNMPKPMLKVAGKPLIEHHINNLKAAdITDIVINlawqgdkIKDYFKDGSQFGVNILYSQEV 80
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVIS-------ANRDQERYALLGVPVIPDEPP 67

                          90       100
                  ....*....|....*....|....*
gi 1741209931  81 EGG-LetaGGIIEALPLLGDSFIVI 104
Cdd:cd02503    68 GKGpL---AGILAALRAAPADWVLV 89
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-51 1.10e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 48.32  E-value: 1.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1741209931   3 AMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVI 51
Cdd:PRK14353    8 AIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAV 53
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-104 2.06e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 46.67  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMMPltqNMPKPMLKVAGKPLIEHHINNLKAADITD---IVINLAWQGDKIKDYFKDGSQFGVnilysqe 79
Cdd:PRK00155    6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPRIDeiiVVVPPDDRPDFAELLLAKDPKVTV------- 75

                          90       100
                  ....*....|....*....|....*
gi 1741209931  80 VEGGLETAGGIIEALPLLGDSFIVI 104
Cdd:PRK00155   76 VAGGAERQDSVLNGLQALPDDDWVL 100
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-31 2.51e-06

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 46.99  E-value: 2.51e-06
                          10        20
                  ....*....|....*....|....*....
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGK 31
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPAVPFGGK 32
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-52 4.23e-06

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 45.57  E-value: 4.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1741209931   1 MKAMILAAGRGQRMmpltqNMPKPMLKVAGKPLIEHHINNLKAAdITDIVIN 52
Cdd:COG0746     5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIV 50
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-52 7.71e-06

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 44.79  E-value: 7.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1741209931   1 MKAMILAAGRGQRMmpltQNMPKPMLKVAGKPLIEHHINNLkAADITDIVIN 52
Cdd:PRK00317    4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIERL-APQVDEIVIN 50
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-135 1.23e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.12  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFkdGSQFGVNILYSQEVEG 82
Cdd:PRK14355    6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHF--AGDGDVSFALQEEQLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1741209931  83 GLETAGGIIEALPLLGDSFIVINGDV--YTDYDVSVLMQLHLQPGEAHIVL---IENP 135
Cdd:PRK14355   81 TGHAVACAAPALDGFSGTVLILCGDVplLRAETLQGMLAAHRATGAAVTVLtarLENP 138
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-46 2.28e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 44.63  E-value: 2.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1741209931   1 MKAMILAAGRGQRMMpltQNMPKPMLKVAGKPLIEHHI---NNLKAADI 46
Cdd:PRK09451    6 MSVVILAAGKGTRMY---SDLPKVLHTLAGKPMVQHVIdaaNELGAQHV 51
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-113 2.54e-05

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: 43.30  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGK-PLIEHHINNLKAADITDIVI----NLAWQGDKI---KDYFKDGSQFGVNI 74
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRyRLIDFPLSNMVNSGIRNVGVltqyKSRSLNDHLgsgKEWDLDRKNGGLFI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1741209931  75 LYSQEVEGG---LETAGGIIEALPLLGDS----FIVINGD-VYT-DYD 113
Cdd:cd02508    81 LPPQQRKGGdwyRGTADAIYQNLDYIERSdpeyVLILSGDhIYNmDYR 128
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-108 9.20e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 42.61  E-value: 9.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   5 ILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHIN---NLKAADITDIVinlAWQGDKIKDYFKDGSqfGVNILYSQEVE 81
Cdd:PRK14360    6 ILAAGKGTRM---KSSLPKVLHPLGGKSLVERVLDsceELKPDRRLVIV---GHQAEEVEQSLAHLP--GLEFVEQQPQL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1741209931  82 GgleTAGGIIEALPLLGD---SFIVINGDV 108
Cdd:PRK14360   78 G---TGHAVQQLLPVLKGfegDLLVLNGDV 104
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 3-99 2.86e-04

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 40.40  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmpltqNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDK-IKDY-FKDGSQFGVNILY---- 76
Cdd:TIGR03310   2 AIILAAGLSSRM-----GQNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADElVALLaNHSNITLVHNPQYaegq 76

                          90       100
                  ....*....|....*....|...
gi 1741209931  77 SQEVEGGLETAGGIIEALPLLGD 99
Cdd:TIGR03310  77 SSSIKLGLELPVQSDGYLFLLGD 99
molyb_mobA TIGR02665
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ...
 3-95 3.28e-04

molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing enzymes, including nitrate reductase and dimethylsulfoxide reductase, the cofactor is molybdopterin-guanine dinucleotide. The family described here contains MobA, molybdenum cofactor guanylyltransferase, from the Proteobacteria only. MobA can reconstitute molybdopterin-guanine dinucleotide biosynthesis without the product of the neighboring gene MobB. The probable MobA proteins of other lineages differ sufficiently that they are not included in scope of this family. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274249  Cd Length: 186  Bit Score: 39.96  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmpltQNMPKPMLKVAGKPLIEHHINNLKaADITDIVINlAWQGDKIKDYFKDGSQfgvniLYSQEVEG 82
Cdd:TIGR02665   3 GVILAGGRARRM----GGRDKGLVELGGKPLIEHVLARLR-PQVSDLAIS-ANRNPERYAQAGFGLP-----VVPDALAD 71

                          90
                  ....*....|...
gi 1741209931  83 GLETAGGIIEALP 95
Cdd:TIGR02665  72 FPGPLAGILAGLR 84
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-108 5.16e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.52  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNLKAadITDIV-INLAWQGDKIKDYFKDgsqfGVNIlYSQE 79
Cdd:PRK14357    1 MRALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKK--VAQKVgVVLGHEAELVKKLLPE----WVKI-FLQE 70

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1741209931  80 VEggLETAGGIIEALPLL--GDSFIVINGDV 108
Cdd:PRK14357   71 EQ--LGTAHAVMCARDFIepGDDLLILYGDV 99
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 3-51 7.43e-04

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 39.83  E-value: 7.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRmmpLTQNMPKPMLKVAGKPLIEHHINNLKAA-DITDIVI 51
Cdd:PRK09382    8 LVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLENLSSApAFKEIVV 54
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 3-132 8.95e-04

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 38.97  E-value: 8.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVInLAWQGDKiKDYFKDgsqfgvnilysqeveg 82
Cdd:pfam01128   1 AVIPAAGSGKRM---GAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIV-VAVSPDD-TPEFRQ---------------- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1741209931  83 gletaggiiealpLLGDSFIVI--NGDVYTDydvSVLMQLHLQPGEAHIVLI 132
Cdd:pfam01128  60 -------------LLGDPSIQLvaGGDTRQD---SVLNGLKALAGTAKFVLV 95
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-75 1.20e-03

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: 39.10  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   1 MKAMILAAGRGQRMMPL-TQNMPKPMLKVAG-KPLIEHHINNLKAADITD---IVINLAwQGDKIKDYFKDGSQfGVNIL 75
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFGdKSLLQQTLDRLKGLVPPDrilVVTNEE-YRFLVREQLPEGLP-EENII 78
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 3-66 1.75e-03

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


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 38.58  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1741209931   3 AMILAAGRGQRMmpltQNMPKPMLKVAGKPLIEHHINNLKAAdITDIVINLAWQGDKIKDYFKD 66
Cdd:PRK14489    8 GVILAGGLSRRM----NGRDKALILLGGKPLIERVVDRLRPQ-FARIHLNINRDPARYQDLFPG 66
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-51 1.97e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 38.65  E-value: 1.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGK-PLIEHHINNLKAADITDIVI 51
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSyRLIDFVLSNLVNSGYLRIYV 57
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-31 2.10e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 38.31  E-value: 2.10e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1741209931   1 MKAMILAAGRGQRMMPLTQNMPKPMLKVAGK 31
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGK 34
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-31 2.21e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 38.28  E-value: 2.21e-03
                          10        20
                  ....*....|....*....|....*....
gi 1741209931   3 AMILAAGRGQRMMPLTQNMPKPMLKVAGK 31
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAVYFGGK 46
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 3.22e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 37.78  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741209931   3 AMILAAGRGQRMmplTQNMPKPMLKVAGKPLIEHHINNLKAADITDIVINLAWQGDKIKDYFKDGSQfgvNILYSQEVEG 82
Cdd:PRK14356    8 ALILAAGKGTRM---HSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDA---RFVLQEQQLG 81

                          90       100
                  ....*....|....*....|....*....
gi 1741209931  83 gleTAGGIIEALPLLG----DSFIVINGD 107
Cdd:PRK14356   82 ---TGHALQCAWPSLTaaglDRVLVVNGD 107
 
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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