|
Name |
Accession |
Description |
Interval |
E-value |
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
7-194 |
1.18e-100 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 288.62 E-value: 1.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 7 ITGVVLAGGRATRMGGEDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHIDIYQRSGFPVYQDNLADFPGPLAGMLSV 86
Cdd:PRK00317 4 ITGVILAGGRSRRMGGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSLADFPGPLAGILAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 87 MQQSQGEWFLFCSCDTPFIPTCLVERMVQ--QRGDSPVVWVHDGERDHPTIALINRSLIPAMSDYLASGERRVMVFMRKV 164
Cdd:PRK00317 84 LKQARTEWVLVVPCDTPFIPPDLVARLAQaaGKDDADVAWAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAFYARH 163
|
170 180 190
....*....|....*....|....*....|
gi 829934793 165 GGHAVDFSDMKTSFVNVNTIEDLQAMQEKR 194
Cdd:PRK00317 164 GGVAVDFSDPKDAFFNINTPEDLAQLEELL 193
|
|
| molyb_mobA |
TIGR02665 |
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
7-188 |
3.39e-87 |
|
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: 254.51 E-value: 3.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 7 ITGVVLAGGRATRMGGEDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHIDIYQRSGF--PVYQDNLADFPGPLAGML 84
Cdd:TIGR02665 1 ISGVILAGGRARRMGGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAGFglPVVPDALADFPGPLAGIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 85 SVMQQSQGEWFLFCSCDTPFIPTCLVERMVQ--QRGDSPVVWVHDGERDHPTIALINRSLIPAMSDYLASGERRVMVFMR 162
Cdd:TIGR02665 81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAalEASDADIAVAHDGGRWHPVFALWPVALAPDLEAFLAAGERRVRRFYA 160
|
170 180
....*....|....*....|....*.
gi 829934793 163 KVGGHAVDFSDMKTSFVNVNTIEDLQ 188
Cdd:TIGR02665 161 RHGAVAVDFSDSPDAFANLNTPEDLA 186
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
6-192 |
2.16e-75 |
|
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: 224.30 E-value: 2.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 6 EITGVVLAGGRATRMGGeDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHiDIYQRSGFPVYQDNLADfPGPLAGMLS 85
Cdd:COG0746 4 PITGVILAGGRSRRMGQ-DKALLPLGGRPLLERVLERLRPQVDEVVIVANRP-ERYAALGVPVVPDDPPG-AGPLAGILA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 86 VMQQSQGEWFLFCSCDTPFIPTCLVERMVQQRG-DSPVVWVHDGERDHPTIALINRSLIPAMSDYLASGERRVMVFMRKV 164
Cdd:COG0746 81 ALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEeGADAVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLERL 160
|
170 180
....*....|....*....|....*...
gi 829934793 165 GGHAVDFSDMKTSFVNVNTIEDLQAMQE 192
Cdd:COG0746 161 DVVYVPFEDLDDAFFNVNTPEDLARAEE 188
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
7-187 |
7.92e-68 |
|
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: 205.12 E-value: 7.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 7 ITGVVLAGGRATRMGGeDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHIDIYQRSGFPVYQDNLaDFPGPLAGMLSV 86
Cdd:cd02503 1 ITGVILAGGKSRRMGG-DKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPDEP-PGKGPLAGILAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 87 MQQSQGEWFLFCSCDTPFIPTCLVERMVQQRGDSP-VVWVHDGERDHPTIALINRSLIPAMSDYLASGERRVMVFMRKVG 165
Cdd:cd02503 79 LRAAPADWVLVLACDMPFLPPELLERLLAAAEEGAdAVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLG 158
|
170 180
....*....|....*....|...
gi 829934793 166 GHAVDFSD-MKTSFVNVNTIEDL 187
Cdd:cd02503 159 VQYVEFEDeRLDAFFNINTPEDL 181
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
9-164 |
3.17e-36 |
|
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: 123.84 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 9 GVVLAGGRATRMGGeDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRH--IDIYQRSGFPVYQDNLADfPGPLAGMLSV 86
Cdd:pfam12804 1 AVILAGGRSSRMGG-DKALLPLGGKPLLERVLERLRPAGDEVVVVANDEevLAALAGLGVPVVPDPDPG-QGPLAGLLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 87 MQQSQG-EWFLFCSCDTPFIPTCLVERMVQQRGDSP---VVWVHDGERDHPtiALINRSLIPAMSDYL-ASGERRVMVFM 161
Cdd:pfam12804 79 LRAAPGaDAVLVLACDMPFLTPELLRRLLAAAEESGadiVVPVYDGGRGHP--LLYRRRLLPALEALLgDRGLRRLLRRL 156
|
...
gi 829934793 162 RKV 164
Cdd:pfam12804 157 DEV 159
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
7-194 |
1.18e-100 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 288.62 E-value: 1.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 7 ITGVVLAGGRATRMGGEDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHIDIYQRSGFPVYQDNLADFPGPLAGMLSV 86
Cdd:PRK00317 4 ITGVILAGGRSRRMGGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSLADFPGPLAGILAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 87 MQQSQGEWFLFCSCDTPFIPTCLVERMVQ--QRGDSPVVWVHDGERDHPTIALINRSLIPAMSDYLASGERRVMVFMRKV 164
Cdd:PRK00317 84 LKQARTEWVLVVPCDTPFIPPDLVARLAQaaGKDDADVAWAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAFYARH 163
|
170 180 190
....*....|....*....|....*....|
gi 829934793 165 GGHAVDFSDMKTSFVNVNTIEDLQAMQEKR 194
Cdd:PRK00317 164 GGVAVDFSDPKDAFFNINTPEDLAQLEELL 193
|
|
| molyb_mobA |
TIGR02665 |
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
7-188 |
3.39e-87 |
|
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: 254.51 E-value: 3.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 7 ITGVVLAGGRATRMGGEDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHIDIYQRSGF--PVYQDNLADFPGPLAGML 84
Cdd:TIGR02665 1 ISGVILAGGRARRMGGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAGFglPVVPDALADFPGPLAGIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 85 SVMQQSQGEWFLFCSCDTPFIPTCLVERMVQ--QRGDSPVVWVHDGERDHPTIALINRSLIPAMSDYLASGERRVMVFMR 162
Cdd:TIGR02665 81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAalEASDADIAVAHDGGRWHPVFALWPVALAPDLEAFLAAGERRVRRFYA 160
|
170 180
....*....|....*....|....*.
gi 829934793 163 KVGGHAVDFSDMKTSFVNVNTIEDLQ 188
Cdd:TIGR02665 161 RHGAVAVDFSDSPDAFANLNTPEDLA 186
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
6-192 |
2.16e-75 |
|
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: 224.30 E-value: 2.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 6 EITGVVLAGGRATRMGGeDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHiDIYQRSGFPVYQDNLADfPGPLAGMLS 85
Cdd:COG0746 4 PITGVILAGGRSRRMGQ-DKALLPLGGRPLLERVLERLRPQVDEVVIVANRP-ERYAALGVPVVPDDPPG-AGPLAGILA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 86 VMQQSQGEWFLFCSCDTPFIPTCLVERMVQQRG-DSPVVWVHDGERDHPTIALINRSLIPAMSDYLASGERRVMVFMRKV 164
Cdd:COG0746 81 ALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEeGADAVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLERL 160
|
170 180
....*....|....*....|....*...
gi 829934793 165 GGHAVDFSDMKTSFVNVNTIEDLQAMQE 192
Cdd:COG0746 161 DVVYVPFEDLDDAFFNVNTPEDLARAEE 188
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
7-187 |
7.92e-68 |
|
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: 205.12 E-value: 7.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 7 ITGVVLAGGRATRMGGeDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHIDIYQRSGFPVYQDNLaDFPGPLAGMLSV 86
Cdd:cd02503 1 ITGVILAGGKSRRMGG-DKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPDEP-PGKGPLAGILAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 87 MQQSQGEWFLFCSCDTPFIPTCLVERMVQQRGDSP-VVWVHDGERDHPTIALINRSLIPAMSDYLASGERRVMVFMRKVG 165
Cdd:cd02503 79 LRAAPADWVLVLACDMPFLPPELLERLLAAAEEGAdAVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLG 158
|
170 180
....*....|....*....|...
gi 829934793 166 GHAVDFSD-MKTSFVNVNTIEDL 187
Cdd:cd02503 159 VQYVEFEDeRLDAFFNINTPEDL 181
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
1-187 |
7.64e-60 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 190.73 E-value: 7.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 1 MNLSlEITGVVLAGGRATRMGGEDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHIDIYQ--RSGFPVYQDNLADFPG 78
Cdd:PRK14489 1 MQIS-QIAGVILAGGLSRRMNGRDKALILLGGKPLIERVVDRLRPQFARIHLNINRDPARYQdlFPGLPVYPDILPGFQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 79 PLAGMLSVMQQSQGEWFLFCSCDTPFIPTCLVERM--VQQRGDSPVVWVHDGERDHPTIALINRSLIPAMSDYLASGERR 156
Cdd:PRK14489 80 PLSGILAGLEHADSEYLFVVACDTPFLPENLVKRLskALAIEGADIAVPHDGERAHPLFALYHRSCLPALRRYLAEGERR 159
|
170 180 190
....*....|....*....|....*....|.
gi 829934793 157 VMVFMRKVGGHAVDFSDMKTSFVNVNTIEDL 187
Cdd:PRK14489 160 LFDFFQRQRVRYVDLSTQKDAFFNVNTPEDL 190
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
9-164 |
3.17e-36 |
|
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: 123.84 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 9 GVVLAGGRATRMGGeDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRH--IDIYQRSGFPVYQDNLADfPGPLAGMLSV 86
Cdd:pfam12804 1 AVILAGGRSSRMGG-DKALLPLGGKPLLERVLERLRPAGDEVVVVANDEevLAALAGLGVPVVPDPDPG-QGPLAGLLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 87 MQQSQG-EWFLFCSCDTPFIPTCLVERMVQQRGDSP---VVWVHDGERDHPtiALINRSLIPAMSDYL-ASGERRVMVFM 161
Cdd:pfam12804 79 LRAAPGaDAVLVLACDMPFLTPELLRRLLAAAEESGadiVVPVYDGGRGHP--LLYRRRLLPALEALLgDRGLRRLLRRL 156
|
...
gi 829934793 162 RKV 164
Cdd:pfam12804 157 DEV 159
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
7-193 |
6.53e-17 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 74.81 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 7 ITGVVLAGGRATRMGGeDKGLQLLKGKPLWQHVADTL----VDQVSAmALSANRH--IDIYQRSGFPVyqdnlADFPGPL 80
Cdd:COG2068 4 VAAIILAAGASSRMGR-PKLLLPLGGKPLLERAVEAAlaagLDPVVV-VLGADAEevAAALAGLGVRV-----VVNPDWE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 81 AGMLSVMQ------QSQGEWFLFCSCDTPFIPTCLVERMVQQRGDSP---VVWVHDGERDHPtiALINRSLIPA------ 145
Cdd:COG2068 77 EGMSSSLRaglaalPADADAVLVLLGDQPLVTAETLRRLLAAFRESPasiVAPTYDGRRGHP--VLFSRRLFPEllaltg 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 829934793 146 ---MSDYLASGERRVmvfmrkvggHAVDFSDmKTSFVNVNTIEDLQAMQEK 193
Cdd:COG2068 155 dqgARALLRRHPDRV---------RLVPVDD-PGVLLDIDTPEDLARLLAR 195
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
7-188 |
1.42e-15 |
|
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: 71.05 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 7 ITGVVLAGGRATRMGGeDKGLQLLKGKPLWQHVADTL----VDQVsAMALSANRHIDIYQRSGFPVyqdNLADFPGPLAG 82
Cdd:cd04182 1 IAAIILAAGRSSRMGG-NKLLLPLDGKPLLRHALDAAlaagLSRV-IVVLGAEADAVRAALAGLPV---VVVINPDWEEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 83 ML-SV---MQQSQGEW--FLFCSCDTPFIPTCLVERMV---QQRGDSPVVWVHDGERDHPtiALINRSLIPAMSDylASG 153
Cdd:cd04182 76 MSsSLaagLEALPADAdaVLILLADQPLVTAETLRALIdafREDGAGIVAPVYQGRRGHP--VLFPRSLFPELLA--LSG 151
|
170 180 190
....*....|....*....|....*....|....*
gi 829934793 154 ERRVMVFMRKVGGHAVDFSDMKTSFVNVNTIEDLQ 188
Cdd:cd04182 152 DKGARSLLRAHPDRVVVEVDDPGVLIDIDTPEDLR 186
|
|
| PRK02726 |
PRK02726 |
molybdenum cofactor guanylyltransferase; |
6-193 |
3.88e-15 |
|
molybdenum cofactor guanylyltransferase;
Pssm-ID: 235063 Cd Length: 200 Bit Score: 70.06 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 6 EITGVVLAGGRATRMGgEDKGLQLLKGKPLWQHVADTlvdqvsAMALSANRHI-----DIYQR---SGFPVYQDNLADfP 77
Cdd:PRK02726 7 NLVALILAGGKSSRMG-QDKALLPWQGVPLLQRVARI------AAACADEVYIitpwpERYQSllpPGCHWLREPPPS-Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 78 GPLAGMLSVMQQSQGEWFLFCSCDTPFIPTCLVERMVQQRGDSP----VVWVHDGERDHPTIALINRSLIPAMSDYLASG 153
Cdd:PRK02726 79 GPLVAFAQGLPQIKTEWVLLLACDLPRLTVDVLQEWLQQLENVPeeaiAALPKQEKGWEPLCGFYRRRCLPSLEQFIQQG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 829934793 154 ERRVMVFMRKVGGHAVDFSDMKTSFvNVNTIEDLQAMQEK 193
Cdd:PRK02726 159 GRSFQGWLAQVPVQELALSDPDMLF-NCNTPEDLATIQGI 197
|
|
| PRK00560 |
PRK00560 |
molybdenum cofactor guanylyltransferase MobA; |
7-189 |
2.82e-14 |
|
molybdenum cofactor guanylyltransferase MobA;
Pssm-ID: 167003 Cd Length: 196 Bit Score: 67.86 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 7 ITGVVLAGGRATRMGgEDKGLQLLKGKP-LWQHVADTLVDQVSAMALSANRhiDIYQRSGfPVYQDNLADFPGPLAGMLS 85
Cdd:PRK00560 9 IPCVILAGGKSSRMG-ENKALLPFGSYSsLLEYQYTRLLKLFKKVYISTKD--KKFEFNA-PFLLEKESDLFSPLFGIIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 86 VMQQSQGEWFLFCSCDTPFIPTCLVERMVQQRGdSPVVWVHDGERDHPTIALINRSLIPAMSDYLASGERRVMVFMRKVG 165
Cdd:PRK00560 85 AFLTLQTPEIFFISVDTPFVSFESIKKLCGKEN-FSVTYAKSPTKEHYLISLWHQSLLNALIYALKTQNYRLSDLVKNTS 163
|
170 180
....*....|....*....|....
gi 829934793 166 GHAVDFSDMKtSFVNVNTIEDLQA 189
Cdd:PRK00560 164 SQAVHFEDEE-EFLNLNTLKDYEL 186
|
|
| PRK14490 |
PRK14490 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ... |
4-117 |
2.99e-14 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional
Pssm-ID: 237728 [Multi-domain] Cd Length: 369 Bit Score: 69.69 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 4 SLEITGVVLAGGRATRMGgEDKGLQLLKGKPLWQHVADTLVDQVSAMALSA-NRHIDIYQRSGFPVYQDNLADFpGPLAG 82
Cdd:PRK14490 172 EVPLSGLVLAGGRSSRMG-SDKALLSYHESNQLVHTAALLRPHCQEVFISCrAEQAEQYRSFGIPLITDSYLDI-GPLGG 249
|
90 100 110
....*....|....*....|....*....|....*
gi 829934793 83 MLSVMQQSQGEWFLFCSCDTPFIPTCLVERMVQQR 117
Cdd:PRK14490 250 LLSAQRHHPDAAWLVVACDLPFLDEATLQQLVEGR 284
|
|
| PRK14500 |
PRK14500 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ... |
9-133 |
1.15e-09 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; Provisional
Pssm-ID: 237734 [Multi-domain] Cd Length: 346 Bit Score: 56.44 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 9 GVVLAGGRATRMGgEDKGLQLLKGKPLWQHVADTLVDQVSAMALSANRHidiyQRSGFPVyqDNLADFP------GPLAG 82
Cdd:PRK14500 163 GLVLTGGKSRRMG-KDKALLNYQGQPHAQYLYDLLAKYCEQVFLSARPS----QWQGTPL--ENLPTLPdrgesvGPISG 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 829934793 83 MLSVMQQSQGEWFLFCSCDTPFIPTCLVERMVQQ-RGDSPVVWVHDGERDHP 133
Cdd:PRK14500 236 ILTALQSYPGVNWLVVACDLAYLNSETVEKLLAHyRQDLVATCYENPDQGFP 287
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
12-188 |
5.87e-09 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 52.97 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 12 LAGGRATRMGGEDKGLQLLKGKPLWQHVADTL----VDQVSAmALSAN----------RHIDIYQRSGfpvyqDN----- 72
Cdd:COG2266 1 MAGGKGTRLGGGEKPLLEICGKPMIDRVIDALeescIDKIYV-AVSPNtpktreylkeRGVEVIETPG-----EGyvedl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 73 ---LADFPGPlagmlsvmqqsqgewFLFCSCDTPFIPTCLVERMVQ--QRGDSPV--VWVhdgerdhpTIALINRSLIPA 145
Cdd:COG2266 75 neaLESISGP---------------VLVVPADLPLLTPEIIDDIIDayLESGKPSltVVV--------PAALKRELGVSP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 829934793 146 MSDYLASGERR---VMVFMRKVGGH--AVDFSDMKTSFVNVNTIEDLQ 188
Cdd:COG2266 132 DTTFEIDGELVptgINIVDGSDGEQeeTNLVLDDPRLALNVNTPEDLK 179
|
|
| PRK00576 |
PRK00576 |
molybdopterin-guanine dinucleotide biosynthesis protein A; Provisional |
78-194 |
1.60e-06 |
|
molybdopterin-guanine dinucleotide biosynthesis protein A; Provisional
Pssm-ID: 234798 Cd Length: 178 Bit Score: 46.33 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829934793 78 GPLAGM---LSVMQQSQGEWFLFCSCDTPFIPTCLVERMVQ--QRGDSPVVWVHDGeRDHPTIALINRSLIPAMSDYLAS 152
Cdd:PRK00576 58 GPLPATgrgLRAAAEAGARLAFVCAVDMPYLTVELIDDLARpaAQTDAEVVLPWDG-RDHYLAAVYRTDLAERVDALVGA 136
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 829934793 153 GERRVMVFMRKVGGHAVDFSDMKtSFVNVNTIEDLQAMQEKR 194
Cdd:PRK00576 137 GERSMRALVDASDAQRIVMPESR-PLTNVNTAADLPAPMQPG 177
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
7-47 |
1.34e-05 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 44.05 E-value: 1.34e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 829934793 7 ITGVVLAGGRATRMGGED-KGLQLLKGKPLWQHVADTL-----VDQV 47
Cdd:cd02516 1 VAAIILAAGSGSRMGADIpKQFLELGGKPVLEHTLEAFlahpaIDEI 47
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
10-47 |
5.69e-05 |
|
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: 42.42 E-value: 5.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 829934793 10 VVLAGGRATRMGGE-DKGLQLLKGKPLWQHVADTL-----VDQV 47
Cdd:COG1211 1 IIPAAGSGSRMGAGiPKQFLPLGGKPVLEHTLEAFlahprIDEI 44
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
10-77 |
1.01e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 41.94 E-value: 1.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 829934793 10 VVLAGGRATRMGGE-DKGLQLLKGKPLWQHVADTlvdqvsAMALSAnRHIDIYQRSGFPVYQDNLADFP 77
Cdd:PRK09451 9 VILAAGKGTRMYSDlPKVLHTLAGKPMVQHVIDA------ANELGA-QHVHLVYGHGGDLLKQTLADEP 70
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
5-43 |
4.56e-03 |
|
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: 37.13 E-value: 4.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 829934793 5 LEITGVVLAGGRATRMGGE-DKGLQLLKGKPLWQHVADTL 43
Cdd:PRK09382 4 SDISLVIVAAGRSTRFSAEvKKQWLRIGGKPLWLHVLENL 43
|
|
|