|
Name |
Accession |
Description |
Interval |
E-value |
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
3-191 |
4.86e-100 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 287.08 E-value: 4.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 3 SEAITGVVLAGGRATRMGGIDKGLQALNGRPLWRHVAEALAPQVDELVISANRHLEQWRASGYPVFRDIQEGYQGPLAGM 82
Cdd:PRK00317 1 MPPITGVILAGGRSRRMGGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSLADFPGPLAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 83 LAVMQQVASPWFVFCPCDTPFIPSFLVERFIQ--QRGDAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRVMVFM 160
Cdd:PRK00317 81 LAGLKQARTEWVLVVPCDTPFIPPDLVARLAQaaGKDDADVAWAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAFY 160
|
170 180 190
....*....|....*....|....*....|.
gi 1747056214 161 RQMGGRPVNFSDVKTAFINVNTLEDLQQMQE 191
Cdd:PRK00317 161 ARHGGVAVDFSDPKDAFFNINTPEDLAQLEE 191
|
|
| molyb_mobA |
TIGR02665 |
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
6-187 |
1.79e-84 |
|
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: 247.58 E-value: 1.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 6 ITGVVLAGGRATRMGGIDKGLQALNGRPLWRHVAEALAPQVDELVISANRHLEQWRAS--GYPVFRDIQEGYQGPLAGML 83
Cdd:TIGR02665 1 ISGVILAGGRARRMGGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAgfGLPVVPDALADFPGPLAGIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 84 AVMQQVASPWFVFCPCDTPFIPSFLVERFIQ--QRGDAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRVMVFMR 161
Cdd:TIGR02665 81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAalEASDADIAVAHDGGRWHPVFALWPVALAPDLEAFLAAGERRVRRFYA 160
|
170 180
....*....|....*....|....*.
gi 1747056214 162 QMGGRPVNFSDVKTAFINVNTLEDLQ 187
Cdd:TIGR02665 161 RHGAVAVDFSDSPDAFANLNTPEDLA 186
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
3-191 |
3.69e-80 |
|
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: 236.63 E-value: 3.69e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 3 SEAITGVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDELVISANRHlEQWRASGYPVFRDIQEGyQGPLAGM 82
Cdd:COG0746 2 TMPITGVILAGGRSRRMGQ-DKALLPLGGRPLLERVLERLRPQVDEVVIVANRP-ERYAALGVPVVPDDPPG-AGPLAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 83 LAVMQQVASPWFVFCPCDTPFIPSFLVERFIQQRG-DAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRVMVFMR 161
Cdd:COG0746 79 LAALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEeGADAVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLE 158
|
170 180 190
....*....|....*....|....*....|
gi 1747056214 162 QMGGRPVNFSDVKTAFINVNTLEDLQQMQE 191
Cdd:COG0746 159 RLDVVYVPFEDLDDAFFNVNTPEDLARAEE 188
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
6-186 |
2.29e-71 |
|
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: 213.98 E-value: 2.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 6 ITGVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDELVISANRHLEQWRASGYPVFRDIQEGyQGPLAGMLAV 85
Cdd:cd02503 1 ITGVILAGGKSRRMGG-DKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPDEPPG-KGPLAGILAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 86 MQQVASPWFVFCPCDTPFIPSFLVERFIQQR-GDAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRVMVFMRQMG 164
Cdd:cd02503 79 LRAAPADWVLVLACDMPFLPPELLERLLAAAeEGADAVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLG 158
|
170 180
....*....|....*....|...
gi 1747056214 165 GRPVNFSDV-KTAFINVNTLEDL 186
Cdd:cd02503 159 VQYVEFEDErLDAFFNINTPEDL 181
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
8-157 |
1.82e-41 |
|
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: 137.33 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 8 GVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDELVISANRH--LEQWRASGYPVFRDIQEGyQGPLAGMLAV 85
Cdd:pfam12804 1 AVILAGGRSSRMGG-DKALLPLGGKPLLERVLERLRPAGDEVVVVANDEevLAALAGLGVPVVPDPDPG-QGPLAGLLAA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1747056214 86 MQQVA-SPWFVFCPCDTPFIPSFLVERFIQQR---GDAPVVWAHDGERDHPAVAlvHRQIIPELEAYL-AHGERRVM 157
Cdd:pfam12804 79 LRAAPgADAVLVLACDMPFLTPELLRRLLAAAeesGADIVVPVYDGGRGHPLLY--RRRLLPALEALLgDRGLRRLL 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
3-191 |
4.86e-100 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 287.08 E-value: 4.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 3 SEAITGVVLAGGRATRMGGIDKGLQALNGRPLWRHVAEALAPQVDELVISANRHLEQWRASGYPVFRDIQEGYQGPLAGM 82
Cdd:PRK00317 1 MPPITGVILAGGRSRRMGGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSLADFPGPLAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 83 LAVMQQVASPWFVFCPCDTPFIPSFLVERFIQ--QRGDAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRVMVFM 160
Cdd:PRK00317 81 LAGLKQARTEWVLVVPCDTPFIPPDLVARLAQaaGKDDADVAWAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAFY 160
|
170 180 190
....*....|....*....|....*....|.
gi 1747056214 161 RQMGGRPVNFSDVKTAFINVNTLEDLQQMQE 191
Cdd:PRK00317 161 ARHGGVAVDFSDPKDAFFNINTPEDLAQLEE 191
|
|
| molyb_mobA |
TIGR02665 |
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
6-187 |
1.79e-84 |
|
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: 247.58 E-value: 1.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 6 ITGVVLAGGRATRMGGIDKGLQALNGRPLWRHVAEALAPQVDELVISANRHLEQWRAS--GYPVFRDIQEGYQGPLAGML 83
Cdd:TIGR02665 1 ISGVILAGGRARRMGGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAgfGLPVVPDALADFPGPLAGIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 84 AVMQQVASPWFVFCPCDTPFIPSFLVERFIQ--QRGDAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRVMVFMR 161
Cdd:TIGR02665 81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAalEASDADIAVAHDGGRWHPVFALWPVALAPDLEAFLAAGERRVRRFYA 160
|
170 180
....*....|....*....|....*.
gi 1747056214 162 QMGGRPVNFSDVKTAFINVNTLEDLQ 187
Cdd:TIGR02665 161 RHGAVAVDFSDSPDAFANLNTPEDLA 186
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
3-191 |
3.69e-80 |
|
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: 236.63 E-value: 3.69e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 3 SEAITGVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDELVISANRHlEQWRASGYPVFRDIQEGyQGPLAGM 82
Cdd:COG0746 2 TMPITGVILAGGRSRRMGQ-DKALLPLGGRPLLERVLERLRPQVDEVVIVANRP-ERYAALGVPVVPDDPPG-AGPLAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 83 LAVMQQVASPWFVFCPCDTPFIPSFLVERFIQQRG-DAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRVMVFMR 161
Cdd:COG0746 79 LAALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEeGADAVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLE 158
|
170 180 190
....*....|....*....|....*....|
gi 1747056214 162 QMGGRPVNFSDVKTAFINVNTLEDLQQMQE 191
Cdd:COG0746 159 RLDVVYVPFEDLDDAFFNVNTPEDLARAEE 188
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
6-186 |
2.29e-71 |
|
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: 213.98 E-value: 2.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 6 ITGVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDELVISANRHLEQWRASGYPVFRDIQEGyQGPLAGMLAV 85
Cdd:cd02503 1 ITGVILAGGKSRRMGG-DKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPDEPPG-KGPLAGILAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 86 MQQVASPWFVFCPCDTPFIPSFLVERFIQQR-GDAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRVMVFMRQMG 164
Cdd:cd02503 79 LRAAPADWVLVLACDMPFLPPELLERLLAAAeEGADAVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLG 158
|
170 180
....*....|....*....|...
gi 1747056214 165 GRPVNFSDV-KTAFINVNTLEDL 186
Cdd:cd02503 159 VQYVEFEDErLDAFFNINTPEDL 181
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
1-188 |
5.62e-62 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 196.13 E-value: 5.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 1 MQSEAITGVVLAGGRATRMGGIDKGLQALNGRPLWRHVAEALAPQVDELVISANRHLEQWR--ASGYPVFRDIQEGYQGP 78
Cdd:PRK14489 1 MQISQIAGVILAGGLSRRMNGRDKALILLGGKPLIERVVDRLRPQFARIHLNINRDPARYQdlFPGLPVYPDILPGFQGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 79 LAGMLAVMQQVASPWFVFCPCDTPFIPSFLVERF--IQQRGDAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRV 156
Cdd:PRK14489 81 LSGILAGLEHADSEYLFVVACDTPFLPENLVKRLskALAIEGADIAVPHDGERAHPLFALYHRSCLPALRRYLAEGERRL 160
|
170 180 190
....*....|....*....|....*....|..
gi 1747056214 157 MVFMRQMGGRPVNFSDVKTAFINVNTLEDLQQ 188
Cdd:PRK14489 161 FDFFQRQRVRYVDLSTQKDAFFNVNTPEDLEQ 192
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
8-157 |
1.82e-41 |
|
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: 137.33 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 8 GVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDELVISANRH--LEQWRASGYPVFRDIQEGyQGPLAGMLAV 85
Cdd:pfam12804 1 AVILAGGRSSRMGG-DKALLPLGGKPLLERVLERLRPAGDEVVVVANDEevLAALAGLGVPVVPDPDPG-QGPLAGLLAA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1747056214 86 MQQVA-SPWFVFCPCDTPFIPSFLVERFIQQR---GDAPVVWAHDGERDHPAVAlvHRQIIPELEAYL-AHGERRVM 157
Cdd:pfam12804 79 LRAAPgADAVLVLACDMPFLTPELLRRLLAAAeesGADIVVPVYDGGRGHPLLY--RRRLLPALEALLgDRGLRRLL 153
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
6-191 |
8.65e-19 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 79.82 E-value: 8.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 6 ITGVVLAGGRATRMGGiDKGLQALNGRPLWRHVAE-ALAPQVDE--LVISANRHLEQWRASGYPV-FRDIQEGYQGPLAG 81
Cdd:COG2068 4 VAAIILAAGASSRMGR-PKLLLPLGGKPLLERAVEaALAAGLDPvvVVLGADAEEVAAALAGLGVrVVVNPDWEEGMSSS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 82 MLAVMQQVASPW--FVFCPCDTPFIPSFLVERFIQQRGDAP---VVWAHDGERDHPavALVHRQIIPELEAylAHGERRV 156
Cdd:COG2068 83 LRAGLAALPADAdaVLVLLGDQPLVTAETLRRLLAAFRESPasiVAPTYDGRRGHP--VLFSRRLFPELLA--LTGDQGA 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1747056214 157 MVFMRQMGG--RPVNFSDvKTAFINVNTLEDLQQMQE 191
Cdd:COG2068 159 RALLRRHPDrvRLVPVDD-PGVLLDIDTPEDLARLLA 194
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
6-187 |
2.46e-18 |
|
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: 78.37 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 6 ITGVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDE---LVISANRHLEQWRASGYPVFRDIQEGYQGPLAGM 82
Cdd:cd04182 1 IAAIILAAGRSSRMGG-NKLLLPLDGKPLLRHALDAALAAGLSrviVVLGAEADAVRAALAGLPVVVVINPDWEEGMSSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 83 LAV-MQQVASPW--FVFCPCDTPFIPSFLVERFI---QQRGDAPVVWAHDGERDHPavALVHRQIIPELEAYLA-HGERR 155
Cdd:cd04182 80 LAAgLEALPADAdaVLILLADQPLVTAETLRALIdafREDGAGIVAPVYQGRRGHP--VLFPRSLFPELLALSGdKGARS 157
|
170 180 190
....*....|....*....|....*....|..
gi 1747056214 156 VmvfMRQMGGRPVNFSDVKTAFINVNTLEDLQ 187
Cdd:cd04182 158 L---LRAHPDRVVVEVDDPGVLIDIDTPEDLR 186
|
|
| PRK02726 |
PRK02726 |
molybdenum cofactor guanylyltransferase; |
5-191 |
2.91e-17 |
|
molybdenum cofactor guanylyltransferase;
Pssm-ID: 235063 Cd Length: 200 Bit Score: 75.84 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 5 AITGVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDELVIsanrhLEQWR-------ASGYPVFRDIQEGyQG 77
Cdd:PRK02726 7 NLVALILAGGKSSRMGQ-DKALLPWQGVPLLQRVARIAAACADEVYI-----ITPWPeryqsllPPGCHWLREPPPS-QG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 78 PLAGMLAVMQQVASPWFVFCPCDTPFIPSFLVERFIQQRGDAP----VVWAHDGERDHPAVALVHRQIIPELEAYLAHGE 153
Cdd:PRK02726 80 PLVAFAQGLPQIKTEWVLLLACDLPRLTVDVLQEWLQQLENVPeeaiAALPKQEKGWEPLCGFYRRRCLPSLEQFIQQGG 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1747056214 154 RRVMVFMRQMGGRPVNFSDVKTAFiNVNTLEDLQQMQE 191
Cdd:PRK02726 160 RSFQGWLAQVPVQELALSDPDMLF-NCNTPEDLATIQG 196
|
|
| PRK00560 |
PRK00560 |
molybdenum cofactor guanylyltransferase MobA; |
6-187 |
1.49e-15 |
|
molybdenum cofactor guanylyltransferase MobA;
Pssm-ID: 167003 Cd Length: 196 Bit Score: 71.33 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 6 ITGVVLAGGRATRMGgIDKGLQALNGRP-LWRHVAEALAPQVDELVISANRHLEQWRAsgyPVFRDIQEGYQGPLAGMLA 84
Cdd:PRK00560 9 IPCVILAGGKSSRMG-ENKALLPFGSYSsLLEYQYTRLLKLFKKVYISTKDKKFEFNA---PFLLEKESDLFSPLFGIIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 85 VMQQVASPWFVFCPCDTPFIpSFLVERFIQQRGDAPVVWAHDGERDHPAVALVHRQIIPELEAYLAHGERRVMVFMRQMG 164
Cdd:PRK00560 85 AFLTLQTPEIFFISVDTPFV-SFESIKKLCGKENFSVTYAKSPTKEHYLISLWHQSLLNALIYALKTQNYRLSDLVKNTS 163
|
170 180
....*....|....*....|...
gi 1747056214 165 GRPVNFSDVKTaFINVNTLEDLQ 187
Cdd:PRK00560 164 SQAVHFEDEEE-FLNLNTLKDYE 185
|
|
| PRK14490 |
PRK14490 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ... |
6-116 |
2.30e-15 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional
Pssm-ID: 237728 [Multi-domain] Cd Length: 369 Bit Score: 72.77 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 6 ITGVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDELVISA-NRHLEQWRASGYPVfrdIQEGYQ--GPLAGM 82
Cdd:PRK14490 175 LSGLVLAGGRSSRMGS-DKALLSYHESNQLVHTAALLRPHCQEVFISCrAEQAEQYRSFGIPL---ITDSYLdiGPLGGL 250
|
90 100 110
....*....|....*....|....*....|....*
gi 1747056214 83 L-AVMQQVASPWFVfCPCDTPFIPSFLVERFIQQR 116
Cdd:PRK14490 251 LsAQRHHPDAAWLV-VACDLPFLDEATLQQLVEGR 284
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
11-187 |
1.16e-13 |
|
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: 66.07 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 11 LAGGRATRMGGIDKGLQALNGRPLWRHVAEALAP-QVDELVISANRH---LEQW-RASGYPVFRDIQEGYqgpLAGMLAV 85
Cdd:COG2266 1 MAGGKGTRLGGGEKPLLEICGKPMIDRVIDALEEsCIDKIYVAVSPNtpkTREYlKERGVEVIETPGEGY---VEDLNEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 86 MQQVASPwFVFCPCDTPFIPSFLVERFIQ--QRGDAPV--VWAhdgerdhpAVALVHRQIIPELEAYLAHGERR---VMV 158
Cdd:COG2266 78 LESISGP-VLVVPADLPLLTPEIIDDIIDayLESGKPSltVVV--------PAALKRELGVSPDTTFEIDGELVptgINI 148
|
170 180 190
....*....|....*....|....*....|..
gi 1747056214 159 FMRQMGGRP---VNFSDVKTAFiNVNTLEDLQ 187
Cdd:COG2266 149 VDGSDGEQEetnLVLDDPRLAL-NVNTPEDLK 179
|
|
| PRK14500 |
PRK14500 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ... |
8-190 |
8.33e-10 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; Provisional
Pssm-ID: 237734 [Multi-domain] Cd Length: 346 Bit Score: 56.83 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 8 GVVLAGGRATRMGGiDKGLQALNGRPLWRHVAEALAPQVDELVISANRHleQWRASGY---PVFRDIQEGYqGPLAGMLA 84
Cdd:PRK14500 163 GLVLTGGKSRRMGK-DKALLNYQGQPHAQYLYDLLAKYCEQVFLSARPS--QWQGTPLenlPTLPDRGESV-GPISGILT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 85 VMQQVASPWFVFCPCDTPFIPSFLVERFIQQ-RGDAPVVWAHDGERDHPAV--ALVHRQIIPELEAYLAHGER-RVMVFM 160
Cdd:PRK14500 239 ALQSYPGVNWLVVACDLAYLNSETVEKLLAHyRQDLVATCYENPDQGFPEAlcAIYTPQALQVFEKAYAEGLYcPVKILQ 318
|
170 180 190
....*....|....*....|....*....|
gi 1747056214 161 RQMGGRPVNFSDVKTAfiNVNTLEDLQQMQ 190
Cdd:PRK14500 319 RAPCQLIKPDNLFDIA--NINTPEEYGQIN 346
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
6-56 |
7.15e-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: 53.30 E-value: 7.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1747056214 6 ITGVVLAGGRATRMG-GIDKGLQALNGRPLWRHVAEALA--PQVDELVISANRH 56
Cdd:cd02516 1 VAAIILAAGSGSRMGaDIPKQFLELGGKPVLEHTLEAFLahPAIDEIVVVVPPD 54
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
9-62 |
7.66e-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: 50.51 E-value: 7.66e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1747056214 9 VVLAGGRATRMG-GIDKGLQALNGRPLWRHVAEALA--PQVDELVISANR-HLEQWRA 62
Cdd:COG1211 1 IIPAAGSGSRMGaGIPKQFLPLGGKPVLEHTLEAFLahPRIDEIVVVVPPdDIEYFEE 58
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
6-122 |
7.29e-06 |
|
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: 45.22 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 6 ITGVVLAGGRATRMG-GIDKGLQALNGRPLWRHVAEAL--APQVDELVISANrhleqwrASGYPVFRDIQEGYQGPLA-- 80
Cdd:PRK09382 6 ISLVIVAAGRSTRFSaEVKKQWLRIGGKPLWLHVLENLssAPAFKEIVVVIH-------PDDIAYMKKALPEIKFVTLvt 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1747056214 81 -------GMLAVMQQVASPwFVFCPcDT--PFIPSFLVERFIQQRGDAPVV 122
Cdd:PRK09382 79 ggatrqeSVRNALEALDSE-YVLIH-DAarPFVPKELIDRLIEALDKADCV 127
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
9-124 |
2.45e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 43.94 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 9 VVLAGGRATRM-GGIDKGLQALNGRPLWRHVAEALAPQVDELVISANRH-LEQWRA-----SGYPVFRDIQEGYQGPLAG 81
Cdd:PRK14356 9 LILAAGKGTRMhSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHrADMVRAafpdeDARFVLQEQQLGTGHALQC 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1747056214 82 MLAVMQQVASPWFVFCPCDTPFIPSFLVERFIQQRGDAPVVWA 124
Cdd:PRK14356 89 AWPSLTAAGLDRVLVVNGDTPLVTTDTIDDFLKEAAGADLAFM 131
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
9-54 |
2.08e-04 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 40.50 E-value: 2.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1747056214 9 VVLAGGRATRMG-GIDKGLQALNGRPLWRHVAEAL--APQVDELVISAN 54
Cdd:PRK00155 7 IIPAAGKGSRMGaDRPKQYLPLGGKPILEHTLEAFlaHPRIDEIIVVVP 55
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
7-59 |
2.70e-03 |
|
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: 37.44 E-value: 2.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1747056214 7 TGVVLAGGRATRMG----GIDKGLQALNGRPLWRHVAEALAPQ-VDELVISANRHLEQ 59
Cdd:COG1208 1 KAVILAGGLGTRLRpltdTRPKPLLPVGGKPLLEHILERLAAAgITEIVINVGYLAEQ 58
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-122 |
4.43e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 37.15 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747056214 1 MQSEAITGVVLAGGRATRM-GGIDKGLQALNGRPLWRHVAEALAP-QVDELVISANRHLEQWRASGYPVFRDIQEGYQGP 78
Cdd:PRK14353 1 MTDRTCLAIILAAGEGTRMkSSLPKVLHPVAGRPMLAHVLAAAASlGPSRVAVVVGPGAEAVAAAAAKIAPDAEIFVQKE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1747056214 79 LAGML-AVMQqvASPWF---------VFcpCDTPFIPSFLVERFIQQRGDAPVV 122
Cdd:PRK14353 81 RLGTAhAVLA--AREALaggygdvlvLY--GDTPLITAETLARLRERLADGADV 130
|
|
| |
