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Conserved domains on  [gi|488290540|ref|WP_002361748|]
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MULTISPECIES: molybdenum cofactor guanylyltransferase [Enterococcus]

Protein Classification

molybdenum cofactor guanylyltransferase( domain architecture ID 10002369)

molybdenum cofactor guanylyltransferase (MobA) catalyzes the guanylation of the molybdenum cofactor using GTP as the source for the GMP moiety to form molybdopterin guanine dinucleotide

EC:  2.7.7.77
Gene Symbol:  mobA
Gene Ontology:  GO:0061603|GO:0005525|GO:0006777|GO:0046872
PubMed:  12719427|10978347|9445404|12691742|10521532
SCOP:  4000697|4000697

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 6-189 1.93e-59

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: 183.85  E-value: 1.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   6 ADCTAVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFpkAFRKCTIIQDMYLGKGPLGGIVT 85
Cdd:COG0746    3 MPITGVILAGGRSRRMGQDKALLPLGGRPLLERVLERLRPQVDEVVIVANRPERY--AALGVPVVPDDPPGAGPLAGILA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  86 AMNYTQKAEVFVIACDIPTFSPKLVYQLASKRGQN-QVTIFDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQEFEHL 164
Cdd:COG0746   81 ALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGaDAVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLERL 160

                        170       180
                 ....*....|....*....|....*.
gi 488290540 165 SVKTVQLSKENQ-LKNVNRKEELSQW 189
Cdd:COG0746  161 DVVYVPFEDLDDaFFNVNTPEDLARA 186
 
Name Accession Description Interval E-value
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 6-189 1.93e-59

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: 183.85  E-value: 1.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   6 ADCTAVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFpkAFRKCTIIQDMYLGKGPLGGIVT 85
Cdd:COG0746    3 MPITGVILAGGRSRRMGQDKALLPLGGRPLLERVLERLRPQVDEVVIVANRPERY--AALGVPVVPDDPPGAGPLAGILA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  86 AMNYTQKAEVFVIACDIPTFSPKLVYQLASKRGQN-QVTIFDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQEFEHL 164
Cdd:COG0746   81 ALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGaDAVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLERL 160

                        170       180
                 ....*....|....*....|....*.
gi 488290540 165 SVKTVQLSKENQ-LKNVNRKEELSQW 189
Cdd:COG0746  161 DVVYVPFEDLDDaFFNVNTPEDLARA 186
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 8-186 1.03e-57

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: 179.31  E-value: 1.03e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   8 CTAVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFPKAFrKCTIIQDMYLGKGPLGGIVTAM 87
Cdd:cd02503    1 ITGVILAGGKSRRMGGDKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALL-GVPVIPDEPPGKGPLAGILAAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  88 NYTQKAEVFVIACDIPTFSPKLVYQLASKRGQN-QVTIFDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQEFEHLSV 166
Cdd:cd02503   80 RAAPADWVLVLACDMPFLPPELLERLLAAAEEGaDAVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLGV 159

                        170       180
                 ....*....|....*....|..
gi 488290540 167 KTVQLSKE--NQLKNVNRKEEL 186
Cdd:cd02503  160 QYVEFEDErlDAFFNINTPEDL 181
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 7-189 1.86e-40

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 135.70  E-value: 1.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   7 DCTAVLLCGGKSSRM-GFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKfpkAFRK--CTIIQDMYLG-KGPLGG 82
Cdd:PRK00317   3 PITGVILAGGRSRRMgGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLA---RYAAfgLPVIPDSLADfPGPLAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  83 IVTAMNYTQKAEVFVIACDIPTFSPKLVYQLASKRGQNQVTI--FDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQE 160
Cdd:PRK00317  80 ILAGLKQARTEWVLVVPCDTPFIPPDLVARLAQAAGKDDADVawAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAF 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 488290540 161 FEHLSVKTVQLSK-ENQLKNVNRKEELSQW 189
Cdd:PRK00317 160 YARHGGVAVDFSDpKDAFFNINTPEDLAQL 189
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 10-144 4.34e-32

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: 113.06  E-value: 4.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   10 AVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFPKAFR-KCTIIQDMYLGKGPLGGIVTAMN 88
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLPLGGKPLLERVLERLRPAGDEVVVVANDEEVLAALAGlGVPVVPDPDPGQGPLAGLLAALR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   89 YTQKAE-VFVIACDIPTFSPKLVYQLASKRGQNQ--VTIFDFEG-RQEPLfgFYRCSCLP 144
Cdd:pfam12804  81 AAPGADaVLVLACDMPFLTPELLRRLLAAAEESGadIVVPVYDGgRGHPL--LYRRRLLP 138
molyb_mobA TIGR02665
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ...
 8-186 6.53e-20

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: 82.33  E-value: 6.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540    8 CTAVLLCGGKSSRM-GFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFPKAFR-KCTIIQDMYLG-KGPLGGIV 84
Cdd:TIGR02665   1 ISGVILAGGRARRMgGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAGfGLPVVPDALADfPGPLAGIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   85 TAMNYTQKAEVFVIACDIPTFSPKLVYQLASKRGQNQVTI---FDFeGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQEF 161
Cdd:TIGR02665  81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAALEASDADIavaHDG-GRWHPVFALWPVALAPDLEAFLAAGERRVRRFY 159

                         170       180
                  ....*....|....*....|....*.
gi 488290540  162 EHLSVKTVQLSKENQ-LKNVNRKEEL 186
Cdd:TIGR02665 160 ARHGAVAVDFSDSPDaFANLNTPEDL 185
 
Name Accession Description Interval E-value
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 6-189 1.93e-59

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: 183.85  E-value: 1.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   6 ADCTAVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFpkAFRKCTIIQDMYLGKGPLGGIVT 85
Cdd:COG0746    3 MPITGVILAGGRSRRMGQDKALLPLGGRPLLERVLERLRPQVDEVVIVANRPERY--AALGVPVVPDDPPGAGPLAGILA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  86 AMNYTQKAEVFVIACDIPTFSPKLVYQLASKRGQN-QVTIFDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQEFEHL 164
Cdd:COG0746   81 ALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGaDAVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLERL 160

                        170       180
                 ....*....|....*....|....*.
gi 488290540 165 SVKTVQLSKENQ-LKNVNRKEELSQW 189
Cdd:COG0746  161 DVVYVPFEDLDDaFFNVNTPEDLARA 186
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 8-186 1.03e-57

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: 179.31  E-value: 1.03e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   8 CTAVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFPKAFrKCTIIQDMYLGKGPLGGIVTAM 87
Cdd:cd02503    1 ITGVILAGGKSRRMGGDKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALL-GVPVIPDEPPGKGPLAGILAAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  88 NYTQKAEVFVIACDIPTFSPKLVYQLASKRGQN-QVTIFDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQEFEHLSV 166
Cdd:cd02503   80 RAAPADWVLVLACDMPFLPPELLERLLAAAEEGaDAVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLGV 159

                        170       180
                 ....*....|....*....|..
gi 488290540 167 KTVQLSKE--NQLKNVNRKEEL 186
Cdd:cd02503  160 QYVEFEDErlDAFFNINTPEDL 181
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 7-189 1.86e-40

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 135.70  E-value: 1.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   7 DCTAVLLCGGKSSRM-GFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKfpkAFRK--CTIIQDMYLG-KGPLGG 82
Cdd:PRK00317   3 PITGVILAGGRSRRMgGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLA---RYAAfgLPVIPDSLADfPGPLAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  83 IVTAMNYTQKAEVFVIACDIPTFSPKLVYQLASKRGQNQVTI--FDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQE 160
Cdd:PRK00317  80 ILAGLKQARTEWVLVVPCDTPFIPPDLVARLAQAAGKDDADVawAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAF 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 488290540 161 FEHLSVKTVQLSK-ENQLKNVNRKEELSQW 189
Cdd:PRK00317 160 YARHGGVAVDFSDpKDAFFNINTPEDLAQL 189
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 10-144 4.34e-32

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: 113.06  E-value: 4.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   10 AVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFPKAFR-KCTIIQDMYLGKGPLGGIVTAMN 88
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLPLGGKPLLERVLERLRPAGDEVVVVANDEEVLAALAGlGVPVVPDPDPGQGPLAGLLAALR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   89 YTQKAE-VFVIACDIPTFSPKLVYQLASKRGQNQ--VTIFDFEG-RQEPLfgFYRCSCLP 144
Cdd:pfam12804  81 AAPGADaVLVLACDMPFLTPELLRRLLAAAEESGadIVVPVYDGgRGHPL--LYRRRLLP 138
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 5-188 4.98e-30

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


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 112.92  E-value: 4.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   5 IADCTAVLLCGGKSSRM-GFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQ-KFPKAFRKCTIIQDMYLG-KGPLG 81
Cdd:PRK14489   3 ISQIAGVILAGGLSRRMnGRDKALILLGGKPLIERVVDRLRPQFARIHLNINRDPaRYQDLFPGLPVYPDILPGfQGPLS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  82 GIVTAMNYTQKAEVFVIACDIPTFSPKLVYQLAS--KRGQNQVTIFDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQ 159
Cdd:PRK14489  83 GILAGLEHADSEYLFVVACDTPFLPENLVKRLSKalAIEGADIAVPHDGERAHPLFALYHRSCLPALRRYLAEGERRLFD 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 488290540 160 EFEHLSVKTVQLSKENQ-LKNVNRKEELSQ 188
Cdd:PRK14489 163 FFQRQRVRYVDLSTQKDaFFNVNTPEDLEQ 192
PRK02726 PRK02726
molybdenum cofactor guanylyltransferase;
9-187 1.26e-23

molybdenum cofactor guanylyltransferase;


Pssm-ID: 235063  Cd Length: 200  Bit Score: 92.40  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   9 TAVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTndsqkfPKAFR-------KCTIIQDMYLGKGPLG 81
Cdd:PRK02726   9 VALILAGGKSSRMGQDKALLPWQGVPLLQRVARIAAACADEVYIIT------PWPERyqsllppGCHWLREPPPSQGPLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  82 GIVTAMNYTQKAEVFVIACDIPTFSPKLV----YQLASKRGQNQVTIFDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQI 157
Cdd:PRK02726  83 AFAQGLPQIKTEWVLLLACDLPRLTVDVLqewlQQLENVPEEAIAALPKQEKGWEPLCGFYRRRCLPSLEQFIQQGGRSF 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 488290540 158 RQEFEHLSVKTVQLSKENQLKNVNRKEELS 187
Cdd:PRK02726 163 QGWLAQVPVQELALSDPDMLFNCNTPEDLA 192
PRK00560 PRK00560
molybdenum cofactor guanylyltransferase MobA;
1-185 4.58e-23

molybdenum cofactor guanylyltransferase MobA;


Pssm-ID: 167003  Cd Length: 196  Bit Score: 90.97  E-value: 4.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   1 MAKIIADCT-AVLLCGGKSSRMGFDKALLKIQGQYVILQ-TAEKLMELFEEVILVTNDSqKFpkAFRKCTIIQDMYLGKG 78
Cdd:PRK00560   1 MKNPMIDNIpCVILAGGKSSRMGENKALLPFGSYSSLLEyQYTRLLKLFKKVYISTKDK-KF--EFNAPFLLEKESDLFS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  79 PLGGIVTAMNYTQKAEVFVIACDIPTFSPKLVYQLASKRGQNqVTIFDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIR 158
Cdd:PRK00560  78 PLFGIINAFLTLQTPEIFFISVDTPFVSFESIKKLCGKENFS-VTYAKSPTKEHYLISLWHQSLLNALIYALKTQNYRLS 156

                        170       180
                 ....*....|....*....|....*..
gi 488290540 159 QEFEHLSVKTVQLSKENQLKNVNRKEE 185
Cdd:PRK00560 157 DLVKNTSSQAVHFEDEEEFLNLNTLKD 183
PRK14490 PRK14490
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ...
 9-188 2.00e-21

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


Pssm-ID: 237728 [Multi-domain]  Cd Length: 369  Bit Score: 89.72  E-value: 2.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   9 TAVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKfpKAFRKCTI--IQDMYLGKGPLGGIVTA 86
Cdd:PRK14490 176 SGLVLAGGRSSRMGSDKALLSYHESNQLVHTAALLRPHCQEVFISCRAEQA--EQYRSFGIplITDSYLDIGPLGGLLSA 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  87 MNYTQKAEVFVIACDIPTFSPKLVYQLASKRGQnqvtiFDF--------EGRQEPLFGFYRC-SCLPTFQKQLAQNNyQI 157
Cdd:PRK14490 254 QRHHPDAAWLVVACDLPFLDEATLQQLVEGRNP-----FRFatafrhpdSGRPEPLCAIYEPkSRLRLLLRHAAGNN-SL 327

                        170       180       190
                 ....*....|....*....|....*....|.
gi 488290540 158 RQEFEHLSVKTVQLSKENQLKNVNRKEELSQ 188
Cdd:PRK14490 328 RSFLATSRIEELEPTDPEALQNINDPEEMDR 358
molyb_mobA TIGR02665
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ...
 8-186 6.53e-20

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: 82.33  E-value: 6.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540    8 CTAVLLCGGKSSRM-GFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFPKAFR-KCTIIQDMYLG-KGPLGGIV 84
Cdd:TIGR02665   1 ISGVILAGGRARRMgGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAGfGLPVVPDALADfPGPLAGIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   85 TAMNYTQKAEVFVIACDIPTFSPKLVYQLASKRGQNQVTI---FDFeGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQEF 161
Cdd:TIGR02665  81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAALEASDADIavaHDG-GRWHPVFALWPVALAPDLEAFLAAGERRVRRFY 159

                         170       180
                  ....*....|....*....|....*.
gi 488290540  162 EHLSVKTVQLSKENQ-LKNVNRKEEL 186
Cdd:TIGR02665 160 ARHGAVAVDFSDSPDaFANLNTPEDL 185
PRK14500 PRK14500
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ...
 11-188 1.36e-14

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


Pssm-ID: 237734 [Multi-domain]  Cd Length: 346  Bit Score: 70.69  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  11 VLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMELFEEVILVTNDSQKFPKAFRKCTIIQDMYLGKGPLGGIVTAMNYT 90
Cdd:PRK14500 164 LVLTGGKSRRMGKDKALLNYQGQPHAQYLYDLLAKYCEQVFLSARPSQWQGTPLENLPTLPDRGESVGPISGILTALQSY 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  91 QKAEVFVIACDIPTFSPKLVYQLASKRGQNQV-TIFDF--EGRQEPLFGFYRCSCLPTFQKQLAQNNYqirQEFEHLSVK 167
Cdd:PRK14500 244 PGVNWLVVACDLAYLNSETVEKLLAHYRQDLVaTCYENpdQGFPEALCAIYTPQALQVFEKAYAEGLY---CPVKILQRA 320

                        170       180
                 ....*....|....*....|....
gi 488290540 168 TVQLSKENQ---LKNVNRKEELSQ 188
Cdd:PRK14500 321 PCQLIKPDNlfdIANINTPEEYGQ 344
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 8-54 2.64e-09

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: 54.10  E-value: 2.64e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 488290540   8 CTAVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMEL-FEEVILVT 54
Cdd:cd04182    1 IAAIILAAGRSSRMGGNKLLLPLDGKPLLRHALDAALAAgLSRVIVVL 48
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-54 3.82e-09

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 53.63  E-value: 3.82e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488290540   1 MAKIiadcTAVLLCGGKSSRMGFDKALLKIQGQYVILQTAEKLMEL-FEEVILVT 54
Cdd:COG2068    1 MSKV----AAIILAAGASSRMGRPKLLLPLGGKPLLERAVEAALAAgLDPVVVVL 51
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-62 2.70e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 45.89  E-value: 2.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488290540   8 CTAVLLCGGKSSRMGFD--KALLKIQGQYVILQTAEKL--MELFEEVILVTN--DSQKFPK 62
Cdd:PRK00155   4 VYAIIPAAGKGSRMGADrpKQYLPLGGKPILEHTLEAFlaHPRIDEIIVVVPpdDRPDFAE 64
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 11-69 5.26e-06

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: 45.12  E-value: 5.26e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488290540  11 VLLCGGKSSRMGFD--KALLKIQGQYVILQTAEKL--MELFEEVILVTN--DSQKFPKAFRKCTI 69
Cdd:COG1211    1 IIPAAGSGSRMGAGipKQFLPLGGKPVLEHTLEAFlaHPRIDEIVVVVPpdDIEYFEELLAKYGI 65
PRK00576 PRK00576
molybdopterin-guanine dinucleotide biosynthesis protein A; Provisional
 21-186 5.85e-05

molybdopterin-guanine dinucleotide biosynthesis protein A; Provisional


Pssm-ID: 234798  Cd Length: 178  Bit Score: 41.71  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  21 MGFDKALLKIQGQYVILqtAEKLMELF----EEVILVTNDSQKFPKAfrKCTIIQDMYLGKGPLggIVTAMNYTQKAE-- 94
Cdd:PRK00576   1 MGRDKATLPLPGGTTTL--VEHVVGIVgqrcAPVFVMAAPGQPLPEL--PAPVLRDELRGLGPL--PATGRGLRAAAEag 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  95 ---VFVIACDIPTFSPKLVYQLA-SKRGQNQVTIFDFEGRQEPLFGFYRCSCLPTFQKQLAQNNYQIRQEFEHLSVKTVQ 170
Cdd:PRK00576  75 arlAFVCAVDMPYLTVELIDDLArPAAQTDAEVVLPWDGRDHYLAAVYRTDLAERVDALVGAGERSMRALVDASDAQRIV 154

                        170
                 ....*....|....*.
gi 488290540 171 LSKENQLKNVNRKEEL 186
Cdd:PRK00576 155 MPESRPLTNVNTAADL 170
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 13-113 1.98e-04

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: 40.26  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  13 LCGGKSSRMGF-DKALLKIQGQYVILQTAEKLMEL-FEEVILVTndSQKFPKaFRKCTIIQDMYLGKGPLGGIVTAMNYT 90
Cdd:COG2266    1 MAGGKGTRLGGgEKPLLEICGKPMIDRVIDALEEScIDKIYVAV--SPNTPK-TREYLKERGVEVIETPGEGYVEDLNEA 77

                         90       100
                 ....*....|....*....|....*.
gi 488290540  91 QKAE---VFVIACDIPTFSPKLVYQL 113
Cdd:COG2266   78 LESIsgpVLVVPADLPLLTPEIIDDI 103
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 10-102 7.82e-04

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: 38.72  E-value: 7.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540  10 AVLLCGGKSSRMG-----FDKALLKIQG----QYVIlqtaEKLMEL-FEEVILVTN-----------DSQKFPKAFRkcT 68
Cdd:cd04181    1 AVILAAGKGTRLRpltdtRPKPLLPIAGkpilEYII----ERLARAgIDEIILVVGylgeqieeyfgDGSKFGVNIE--Y 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488290540  69 IIQDMYLGKGplGGIVTAMNYTQKAEVFVIACDI 102
Cdd:cd04181   75 VVQEEPLGTA--GAVRNAEDFLGDDDFLVVNGDV 106
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 9-102 8.25e-04

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: 38.98  E-value: 8.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290540   9 TAVLLCGGKSSRMG-----FDKALLKIQGQYVIlqtaEKLMEL-----FEEVILVTN-----------DSQKFPKAFRkc 67
Cdd:COG1208    1 KAVILAGGLGTRLRpltdtRPKPLLPVGGKPLL----EHILERlaaagITEIVINVGylaeqieeyfgDGSRFGVRIT-- 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488290540  68 TIIQDMYLGKGplGGIVTAMNYTQKAEVFVIACDI 102
Cdd:COG1208   75 YVDEGEPLGTG--GALKRALPLLGDEPFLVLNGDI 107
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 10-55 9.57e-03

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: 35.67  E-value: 9.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488290540  10 AVLLCGGKSSRMG-----FDKALLKIQGQYVILQTAEKLMEL-FEEVILVTN 55
Cdd:cd02523    1 AIILAAGRGSRLRpltedRPKCLLEINGKPLLERQIETLKEAgIDDIVIVTG 52
 
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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