NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1085035287|gb|OGS39779|]
View 

bifunctional adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase [Elusimicrobia bacterium RIFOXYD2_FULL_34_30]

Protein Classification

bifunctional adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase( domain architecture ID 10005279)

bifunctional adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase catalyzes the ATP-dependent phosphorylation of adenosylcobinamide to form adenosylcobinamide phosphate and the addition of guanosine monophosphate to adenosylcobinamide phosphate to form adenosylcobinamide-GDP

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CobU COG2087
Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme ...
 3-171 1.22e-72

Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme transport and metabolism]; Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


:

Pssm-ID: 441690  Cd Length: 172  Bit Score: 215.76  E-value: 1.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   3 KIIFISGGVRSGKSAFALELAQKS-KDVVFIATAgRKEDKEMNKRIEVHQKSRPTHWKTIEETEDIIKHLKALEKA-DCV 80
Cdd:COG2087     1 MLTLVLGGARSGKSRFAEKLAAASgKPVVYIATA-QAFDEEMAERIARHRARRPAGWTTVEEPLDLAAALAALAPPgDVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287  81 IVDCITFLVSNWMF--KKLNEEKIIENMQNIIKKLRKVRGKIIMVSNEVGMGVVPPYKLGRDFRDVIGRVNQLIVKNSNE 158
Cdd:COG2087    80 LVDCLTLWLTNLLFaeDAWEEEDVEAEIDELLEALRALPGPVVLVSNEVGLGIVPENPLGRRFRDLLGRLNQRLAAAADE 159

                         170
                  ....*....|...
gi 1085035287 159 FYFFISGIKWRLK 171
Cdd:COG2087   160 VYLVVAGLPLKLK 172
 
Name Accession Description Interval E-value
CobU COG2087
Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme ...
 3-171 1.22e-72

Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme transport and metabolism]; Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441690  Cd Length: 172  Bit Score: 215.76  E-value: 1.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   3 KIIFISGGVRSGKSAFALELAQKS-KDVVFIATAgRKEDKEMNKRIEVHQKSRPTHWKTIEETEDIIKHLKALEKA-DCV 80
Cdd:COG2087     1 MLTLVLGGARSGKSRFAEKLAAASgKPVVYIATA-QAFDEEMAERIARHRARRPAGWTTVEEPLDLAAALAALAPPgDVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287  81 IVDCITFLVSNWMF--KKLNEEKIIENMQNIIKKLRKVRGKIIMVSNEVGMGVVPPYKLGRDFRDVIGRVNQLIVKNSNE 158
Cdd:COG2087    80 LVDCLTLWLTNLLFaeDAWEEEDVEAEIDELLEALRALPGPVVLVSNEVGLGIVPENPLGRRFRDLLGRLNQRLAAAADE 159

                         170
                  ....*....|...
gi 1085035287 159 FYFFISGIKWRLK 171
Cdd:COG2087   160 VYLVVAGLPLKLK 172
CobU pfam02283
Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group ...
 5-166 9.04e-72

Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group of bifunctional cobalamin biosynthesis enzymes which display cobinamide kinase and cobinamide phosphate guanyltransferase activity. The crystal structure of the enzyme reveals the molecule to be a trimer with a propeller-like shape.


Pssm-ID: 426697  Cd Length: 167  Bit Score: 213.50  E-value: 9.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   5 IFISGGVRSGKSAFALELA-QKSKDVVFIATAgRKEDKEMNKRIEVHQKSRPTHWKTIEETEDIIKHLKALEKADCVIVD 83
Cdd:pfam02283   1 ILVTGGARSGKSRFAERLAlASGGPVVYIATA-QAFDEEMAERIARHRARRPAHWTTIEEPLDLAEALREAPGPDVVLVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287  84 CITFLVSNWMFKK-LNEEKIIENMQNIIKKLRKVRGKIIMVSNEVGMGVVPPYKLGRDFRDVIGRVNQLIVKNSNEFYFF 162
Cdd:pfam02283  80 CLTLWLTNLLLADdGEEEDIEAEVDELLAALKQLPAPVILVSNEVGMGIVPENALGRRFRDLLGRLNQRLAAAADEVYLV 159


                  ....
gi 1085035287 163 ISGI 166
Cdd:pfam02283 160 VAGI 163
CobU cd00544
Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a ...
 5-166 1.10e-67

Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a bacterial bifunctional cobalbumin biosynthesis enzyme which display adenosylcobinamide kinase and adenosylcobinamide phosphate guanyltransferase activity and is a key participant in the final stages of cobalamin biosynthesis where it is involved in nucleotide loop assembly. CobU is a homotrimer which functions both as a kinase and as a nucleotidyl transferase. It phosphorylates of adenosylcobinamide to form adenosylcobinamide phosphate (using a variety of nucleotides as the phosphate donor) and then adds GMP to adenosylcobinamide phosphate to form adenosylcobinamide-GDP, specifically using GTP.


Pssm-ID: 410861  Cd Length: 166  Bit Score: 203.15  E-value: 1.10e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   5 IFISGGVRSGKSAFALELAQKS-KDVVFIATAgRKEDKEMNKRIEVHQKSRPTHWKTIEETEDIIKHLKALEKADCVIVD 83
Cdd:cd00544     1 ILVTGGARSGKSRFAERLALQSgKDVVYVATA-EAFDDEMAERIERHRKRRPAGWQTVEEPLDLAEALRALPKGSVVLLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287  84 CITFLVSNWMFKKLN--EEKIIENMQNIIKKLRKVRGKIIMVSNEVGMGVVPPYKLGRDFRDVIGRVNQLIVKNSNEFYF 161
Cdd:cd00544    80 CLTLWLTNLLFADDGwvEAAIEEEIEALLEALKACPATLIIVSNEVGWGIVPENPLGRRFRDLLGRLNQRLAAAADEVYL 159


                  ....*
gi 1085035287 162 FISGI 166
Cdd:cd00544   160 VVAGI 164
cobU PRK05800
adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; Validated
 2-171 6.58e-65

adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; Validated


Pssm-ID: 235612  Cd Length: 170  Bit Score: 196.16  E-value: 6.58e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   2 GKIIFISGGVRSGKSAFALELAQKS-KDVVFIATAgRKEDKEMNKRIEVHQKSRPTHWKTIEETEDIIKHLKALEKAD-C 79
Cdd:PRK05800    1 GMLILVTGGARSGKSRFAERLAAQSgLQVLYIATA-QPFDDEMAARIAHHRQRRPAHWQTVEEPLDLAELLRADAAPGrC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287  80 VIVDCITFLVSNWMFKKlNEEKIIENMQNIIKKLRKVRGKIIMVSNEVGMGVVPPYKLGRDFRDVIGRVNQLIVKNSNEF 159
Cdd:PRK05800   80 VLVDCLTTWVTNLLFEE-GEEAIAAEIDALLAALQQLPAKIILVTNEVGMGIVPEYRLGRHFRDIAGRLNQQLAAAADEV 158

                         170
                  ....*....|..
gi 1085035287 160 YFFISGIKWRLK 171
Cdd:PRK05800  159 YLVVAGLPLKLK 170
 
Name Accession Description Interval E-value
CobU COG2087
Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme ...
 3-171 1.22e-72

Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme transport and metabolism]; Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441690  Cd Length: 172  Bit Score: 215.76  E-value: 1.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   3 KIIFISGGVRSGKSAFALELAQKS-KDVVFIATAgRKEDKEMNKRIEVHQKSRPTHWKTIEETEDIIKHLKALEKA-DCV 80
Cdd:COG2087     1 MLTLVLGGARSGKSRFAEKLAAASgKPVVYIATA-QAFDEEMAERIARHRARRPAGWTTVEEPLDLAAALAALAPPgDVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287  81 IVDCITFLVSNWMF--KKLNEEKIIENMQNIIKKLRKVRGKIIMVSNEVGMGVVPPYKLGRDFRDVIGRVNQLIVKNSNE 158
Cdd:COG2087    80 LVDCLTLWLTNLLFaeDAWEEEDVEAEIDELLEALRALPGPVVLVSNEVGLGIVPENPLGRRFRDLLGRLNQRLAAAADE 159

                         170
                  ....*....|...
gi 1085035287 159 FYFFISGIKWRLK 171
Cdd:COG2087   160 VYLVVAGLPLKLK 172
CobU pfam02283
Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group ...
 5-166 9.04e-72

Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group of bifunctional cobalamin biosynthesis enzymes which display cobinamide kinase and cobinamide phosphate guanyltransferase activity. The crystal structure of the enzyme reveals the molecule to be a trimer with a propeller-like shape.


Pssm-ID: 426697  Cd Length: 167  Bit Score: 213.50  E-value: 9.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   5 IFISGGVRSGKSAFALELA-QKSKDVVFIATAgRKEDKEMNKRIEVHQKSRPTHWKTIEETEDIIKHLKALEKADCVIVD 83
Cdd:pfam02283   1 ILVTGGARSGKSRFAERLAlASGGPVVYIATA-QAFDEEMAERIARHRARRPAHWTTIEEPLDLAEALREAPGPDVVLVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287  84 CITFLVSNWMFKK-LNEEKIIENMQNIIKKLRKVRGKIIMVSNEVGMGVVPPYKLGRDFRDVIGRVNQLIVKNSNEFYFF 162
Cdd:pfam02283  80 CLTLWLTNLLLADdGEEEDIEAEVDELLAALKQLPAPVILVSNEVGMGIVPENALGRRFRDLLGRLNQRLAAAADEVYLV 159


                  ....
gi 1085035287 163 ISGI 166
Cdd:pfam02283 160 VAGI 163
CobU cd00544
Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a ...
 5-166 1.10e-67

Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a bacterial bifunctional cobalbumin biosynthesis enzyme which display adenosylcobinamide kinase and adenosylcobinamide phosphate guanyltransferase activity and is a key participant in the final stages of cobalamin biosynthesis where it is involved in nucleotide loop assembly. CobU is a homotrimer which functions both as a kinase and as a nucleotidyl transferase. It phosphorylates of adenosylcobinamide to form adenosylcobinamide phosphate (using a variety of nucleotides as the phosphate donor) and then adds GMP to adenosylcobinamide phosphate to form adenosylcobinamide-GDP, specifically using GTP.


Pssm-ID: 410861  Cd Length: 166  Bit Score: 203.15  E-value: 1.10e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   5 IFISGGVRSGKSAFALELAQKS-KDVVFIATAgRKEDKEMNKRIEVHQKSRPTHWKTIEETEDIIKHLKALEKADCVIVD 83
Cdd:cd00544     1 ILVTGGARSGKSRFAERLALQSgKDVVYVATA-EAFDDEMAERIERHRKRRPAGWQTVEEPLDLAEALRALPKGSVVLLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287  84 CITFLVSNWMFKKLN--EEKIIENMQNIIKKLRKVRGKIIMVSNEVGMGVVPPYKLGRDFRDVIGRVNQLIVKNSNEFYF 161
Cdd:cd00544    80 CLTLWLTNLLFADDGwvEAAIEEEIEALLEALKACPATLIIVSNEVGWGIVPENPLGRRFRDLLGRLNQRLAAAADEVYL 159


                  ....*
gi 1085035287 162 FISGI 166
Cdd:cd00544   160 VVAGI 164
cobU PRK05800
adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; Validated
 2-171 6.58e-65

adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; Validated


Pssm-ID: 235612  Cd Length: 170  Bit Score: 196.16  E-value: 6.58e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   2 GKIIFISGGVRSGKSAFALELAQKS-KDVVFIATAgRKEDKEMNKRIEVHQKSRPTHWKTIEETEDIIKHLKALEKAD-C 79
Cdd:PRK05800    1 GMLILVTGGARSGKSRFAERLAAQSgLQVLYIATA-QPFDDEMAARIAHHRQRRPAHWQTVEEPLDLAELLRADAAPGrC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287  80 VIVDCITFLVSNWMFKKlNEEKIIENMQNIIKKLRKVRGKIIMVSNEVGMGVVPPYKLGRDFRDVIGRVNQLIVKNSNEF 159
Cdd:PRK05800   80 VLVDCLTTWVTNLLFEE-GEEAIAAEIDALLAALQQLPAKIILVTNEVGMGIVPEYRLGRHFRDIAGRLNQQLAAAADEV 158

                         170
                  ....*....|..
gi 1085035287 160 YFFISGIKWRLK 171
Cdd:PRK05800  159 YLVVAGLPLKLK 170
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
2-126 1.46e-04

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 40.67  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035287   2 GKIIFISGGVRSGKSAFAL----ELAQKSKDVVFIATAGRKED--KEM------------NKRIEVHQKSRPTHWKTIEE 63
Cdd:COG0467    20 GSSTLLSGPPGTGKTTLALqflaEGLRRGEKGLYVSFEESPEQllRRAeslgldleeyieSGLLRIIDLSPEELGLDLEE 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085035287  64 TEDIIKHLKALEKADCVIVDCITFLVSNWMfkklNEEKIIENMQNIIKKLRKVRGKIIMVSNE 126
Cdd:COG0467   100 LLARLREAVEEFGAKRVVIDSLSGLLLALP----DPERLREFLHRLLRYLKKRGVTTLLTSET 158
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH