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Conserved domains on  [gi|500112359|ref|WP_011788364|]
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MULTISPECIES: bifunctional adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase [Shewanella]

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

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List of domain hits

 Name Accession Description Interval E-value
CobU COG2087
Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme ...
 1-201 2.68e-79

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: 234.25  E-value: 2.68e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359   1 MIHLVVGGARSGKSRYGESLVRQytaLGFDACFVATAQARDAEMTERIVKHQQDRADDgiaWQLIEEPLALTTQLKHLAK 80
Cdd:COG2087    1 MLTLVLGGARSGKSRFAEKLAAA---SGKPVVYIATAQAFDEEMAERIARHRARRPAG---WTTVEEPLDLAAALAALAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359  81 PGRVILVDCLTLWLTNQLLACYPELDEPiptegyfaadiatkntsldplisWQNEKNAFVDSLAELEGVVILISNEVGSG 160
Cdd:COG2087   75 PGDVVLVDCLTLWLTNLLFAEDAWEEED-----------------------VEAEIDELLEALRALPGPVVLVSNEVGLG 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500112359 161 IVPLGALSRQFVDEAGWLNQAVATLADNVTLVVAGLPLTLK 201
Cdd:COG2087  132 IVPENPLGRRFRDLLGRLNQRLAAAADEVYLVVAGLPLKLK 172
 
Name Accession Description Interval E-value
CobU COG2087
Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme ...
 1-201 2.68e-79

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: 234.25  E-value: 2.68e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359   1 MIHLVVGGARSGKSRYGESLVRQytaLGFDACFVATAQARDAEMTERIVKHQQDRADDgiaWQLIEEPLALTTQLKHLAK 80
Cdd:COG2087    1 MLTLVLGGARSGKSRFAEKLAAA---SGKPVVYIATAQAFDEEMAERIARHRARRPAG---WTTVEEPLDLAAALAALAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359  81 PGRVILVDCLTLWLTNQLLACYPELDEPiptegyfaadiatkntsldplisWQNEKNAFVDSLAELEGVVILISNEVGSG 160
Cdd:COG2087   75 PGDVVLVDCLTLWLTNLLFAEDAWEEED-----------------------VEAEIDELLEALRALPGPVVLVSNEVGLG 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500112359 161 IVPLGALSRQFVDEAGWLNQAVATLADNVTLVVAGLPLTLK 201
Cdd:COG2087  132 IVPENPLGRRFRDLLGRLNQRLAAAADEVYLVVAGLPLKLK 172
cobU PRK05800
adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; Validated
 1-201 6.24e-70

adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; Validated


Pssm-ID: 235612  Cd Length: 170  Bit Score: 210.42  E-value: 6.24e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359   1 MIHLVVGGARSGKSRYGESLVRQytaLGFDACFVATAQARDAEMTERIVKHQQDRADDgiaWQLIEEPLALTTQLKHLAK 80
Cdd:PRK05800   2 MLILVTGGARSGKSRFAERLAAQ---SGLQVLYIATAQPFDDEMAARIAHHRQRRPAH---WQTVEEPLDLAELLRADAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359  81 PGRVILVDCLTLWLTNqLLACYPELDepiptegyfaadiatkntsldplisWQNEKNAFVDSLAELEGVVILISNEVGSG 160
Cdd:PRK05800  76 PGRCVLVDCLTTWVTN-LLFEEGEEA-------------------------IAAEIDALLAALQQLPAKIILVTNEVGMG 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500112359 161 IVPLGALSRQFVDEAGWLNQAVATLADNVTLVVAGLPLTLK 201
Cdd:PRK05800 130 IVPEYRLGRHFRDIAGRLNQQLAAAADEVYLVVAGLPLKLK 170
CobU pfam02283
Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group ...
 4-200 8.82e-68

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: 204.64  E-value: 8.82e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359    4 LVVGGARSGKSRYGESLVRQYTAlgfDACFVATAQARDAEMTERIVKHQQDRADDgiaWQLIEEPLALTTQLKHLAKPgR 83
Cdd:pfam02283   2 LVTGGARSGKSRFAERLALASGG---PVVYIATAQAFDEEMAERIARHRARRPAH---WTTIEEPLDLAEALREAPGP-D 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359   84 VILVDCLTLWLTNQLLACYPELDEpiptegyfaadiatkntsldplisWQNEKNAFVDSLAELEGVVILISNEVGSGIVP 163
Cdd:pfam02283  75 VVLVDCLTLWLTNLLLADDGEEED------------------------IEAEVDELLAALKQLPAPVILVSNEVGMGIVP 130

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 500112359  164 LGALSRQFVDEAGWLNQAVATLADNVTLVVAGLPLTL 200
Cdd:pfam02283 131 ENALGRRFRDLLGRLNQRLAAAADEVYLVVAGIPLKL 167
CobU cd00544
Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a ...
 3-198 2.81e-66

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: 200.84  E-value: 2.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359   3 HLVVGGARSGKSRYGESLVRQytaLGFDACFVATAQARDAEMTERIVKHQQDRADDgiaWQLIEEPLALTTQLKHLAKpG 82
Cdd:cd00544    1 ILVTGGARSGKSRFAERLALQ---SGKDVVYVATAEAFDDEMAERIERHRKRRPAG---WQTVEEPLDLAEALRALPK-G 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359  83 RVILVDCLTLWLTNQLLACYPELDEpiptegyfaadiatkntsldpliSWQNEKNAFVDSLAELEGVVILISNEVGSGIV 162
Cdd:cd00544   74 SVVLLDCLTLWLTNLLFADDGWVEA-----------------------AIEEEIEALLEALKACPATLIIVSNEVGWGIV 130

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 500112359 163 PLGALSRQFVDEAGWLNQAVATLADNVTLVVAGLPL 198
Cdd:cd00544  131 PENPLGRRFRDLLGRLNQRLAAAADEVYLVVAGIPL 166
 
Name Accession Description Interval E-value
CobU COG2087
Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme ...
 1-201 2.68e-79

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: 234.25  E-value: 2.68e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359   1 MIHLVVGGARSGKSRYGESLVRQytaLGFDACFVATAQARDAEMTERIVKHQQDRADDgiaWQLIEEPLALTTQLKHLAK 80
Cdd:COG2087    1 MLTLVLGGARSGKSRFAEKLAAA---SGKPVVYIATAQAFDEEMAERIARHRARRPAG---WTTVEEPLDLAAALAALAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359  81 PGRVILVDCLTLWLTNQLLACYPELDEPiptegyfaadiatkntsldplisWQNEKNAFVDSLAELEGVVILISNEVGSG 160
Cdd:COG2087   75 PGDVVLVDCLTLWLTNLLFAEDAWEEED-----------------------VEAEIDELLEALRALPGPVVLVSNEVGLG 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500112359 161 IVPLGALSRQFVDEAGWLNQAVATLADNVTLVVAGLPLTLK 201
Cdd:COG2087  132 IVPENPLGRRFRDLLGRLNQRLAAAADEVYLVVAGLPLKLK 172
cobU PRK05800
adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; Validated
 1-201 6.24e-70

adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; Validated


Pssm-ID: 235612  Cd Length: 170  Bit Score: 210.42  E-value: 6.24e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359   1 MIHLVVGGARSGKSRYGESLVRQytaLGFDACFVATAQARDAEMTERIVKHQQDRADDgiaWQLIEEPLALTTQLKHLAK 80
Cdd:PRK05800   2 MLILVTGGARSGKSRFAERLAAQ---SGLQVLYIATAQPFDDEMAARIAHHRQRRPAH---WQTVEEPLDLAELLRADAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359  81 PGRVILVDCLTLWLTNqLLACYPELDepiptegyfaadiatkntsldplisWQNEKNAFVDSLAELEGVVILISNEVGSG 160
Cdd:PRK05800  76 PGRCVLVDCLTTWVTN-LLFEEGEEA-------------------------IAAEIDALLAALQQLPAKIILVTNEVGMG 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500112359 161 IVPLGALSRQFVDEAGWLNQAVATLADNVTLVVAGLPLTLK 201
Cdd:PRK05800 130 IVPEYRLGRHFRDIAGRLNQQLAAAADEVYLVVAGLPLKLK 170
CobU pfam02283
Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group ...
 4-200 8.82e-68

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: 204.64  E-value: 8.82e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359    4 LVVGGARSGKSRYGESLVRQYTAlgfDACFVATAQARDAEMTERIVKHQQDRADDgiaWQLIEEPLALTTQLKHLAKPgR 83
Cdd:pfam02283   2 LVTGGARSGKSRFAERLALASGG---PVVYIATAQAFDEEMAERIARHRARRPAH---WTTIEEPLDLAEALREAPGP-D 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359   84 VILVDCLTLWLTNQLLACYPELDEpiptegyfaadiatkntsldplisWQNEKNAFVDSLAELEGVVILISNEVGSGIVP 163
Cdd:pfam02283  75 VVLVDCLTLWLTNLLLADDGEEED------------------------IEAEVDELLAALKQLPAPVILVSNEVGMGIVP 130

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 500112359  164 LGALSRQFVDEAGWLNQAVATLADNVTLVVAGLPLTL 200
Cdd:pfam02283 131 ENALGRRFRDLLGRLNQRLAAAADEVYLVVAGIPLKL 167
CobU cd00544
Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a ...
 3-198 2.81e-66

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: 200.84  E-value: 2.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359   3 HLVVGGARSGKSRYGESLVRQytaLGFDACFVATAQARDAEMTERIVKHQQDRADDgiaWQLIEEPLALTTQLKHLAKpG 82
Cdd:cd00544    1 ILVTGGARSGKSRFAERLALQ---SGKDVVYVATAEAFDDEMAERIERHRKRRPAG---WQTVEEPLDLAEALRALPK-G 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500112359  83 RVILVDCLTLWLTNQLLACYPELDEpiptegyfaadiatkntsldpliSWQNEKNAFVDSLAELEGVVILISNEVGSGIV 162
Cdd:cd00544   74 SVVLLDCLTLWLTNLLFADDGWVEA-----------------------AIEEEIEALLEALKACPATLIIVSNEVGWGIV 130

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 500112359 163 PLGALSRQFVDEAGWLNQAVATLADNVTLVVAGLPL 198
Cdd:cd00544  131 PENPLGRRFRDLLGRLNQRLAAAADEVYLVVAGIPL 166
 
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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