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Conserved domains on  [gi|829934793|ref|WP_047366770|]
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MULTISPECIES: molybdenum cofactor guanylyltransferase MobA [Enterobacter]

Protein Classification

molybdenum cofactor guanylyltransferase( domain architecture ID 10791899)

molybdenum cofactor guanylyltransferase catalyzes the guanylation of the molybdenum cofactor

EC:  2.7.7.77
Gene Symbol:  mobA
PubMed:  9445404|12691742
SCOP:  4000697

Graphical summary

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List of domain hits

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
 
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
 
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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