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Conserved domains on  [gi|767974050|ref|XP_011536571|]
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corrinoid adenosyltransferase MMAB isoform X3 [Homo sapiens]

Protein Classification

ATP:cob(I)alamin adenosyltransferase( domain architecture ID 10487543)

ATP:cob(I)alamin adenosyltransferase catalyzes the final step in the conversion of cyanocobalamin (vitamin B12) to adenosylcobalamin, catalyzing the transfer of the adenosyl moiety from ATP to cobalamin

EC:  2.5.1.17
Gene Ontology:  GO:0008817|GO:0031419|GO:0009235|GO:0005524
PubMed:  11160088
SCOP:  4003724

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cob_adeno_trans pfam01923
Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene ...
 5-135 3.45e-53

Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene products of PduO and EutT which are both cobalamin adenosyltransferases. PduO is a protein with ATP:cob(I)alamin adenosyltransferase activity. The main role of this protein is the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation.The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12.


:

Pssm-ID: 460384  Cd Length: 163  Bit Score: 165.75  E-value: 3.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974050    5 GFALELVTEkgHTFAEELQKIQCTLQDVGSALATPCSSAREahlkyTTFKAGPILELEQWIDKYTSQLPPLTAFILPSGG 84
Cdd:pfam01923  39 GLARALLPD--EDLRELLERIQNDLFDLGADLATPGPKEPK-----LRITEEDVERLEKEIDEYNAELPPLKSFILPGGS 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767974050   85 KISSALHFCRAVCRRAERRVVPLVQM-GETDANVAKFLNRLSDYLFTLARYA 135
Cdd:pfam01923 112 PAAAALHVARTVCRRAERRAVALAEEeEEAVRDVLKYLNRLSDLLFVLARYA 163
 
Name Accession Description Interval E-value
Cob_adeno_trans pfam01923
Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene ...
 5-135 3.45e-53

Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene products of PduO and EutT which are both cobalamin adenosyltransferases. PduO is a protein with ATP:cob(I)alamin adenosyltransferase activity. The main role of this protein is the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation.The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12.


Pssm-ID: 460384  Cd Length: 163  Bit Score: 165.75  E-value: 3.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974050    5 GFALELVTEkgHTFAEELQKIQCTLQDVGSALATPCSSAREahlkyTTFKAGPILELEQWIDKYTSQLPPLTAFILPSGG 84
Cdd:pfam01923  39 GLARALLPD--EDLRELLERIQNDLFDLGADLATPGPKEPK-----LRITEEDVERLEKEIDEYNAELPPLKSFILPGGS 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767974050   85 KISSALHFCRAVCRRAERRVVPLVQM-GETDANVAKFLNRLSDYLFTLARYA 135
Cdd:pfam01923 112 PAAAALHVARTVCRRAERRAVALAEEeEEAVRDVLKYLNRLSDLLFVLARYA 163
PduO COG2096
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin ...
 18-146 4.04e-51

Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441699  Cd Length: 180  Bit Score: 161.06  E-value: 4.04e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974050  18 FAEELQKIQCTLQDVGSALATPcsSAREAHLKYTtfkAGPILELEQWIDKYTSQLPPLTAFILPSGGKISSALHFCRAVC 97
Cdd:COG2096   53 LRELLERIQNDLFDLGADLATP--GEKRPPLRIT---EEDVERLEEEIDELNAELPPLKSFILPGGSPAAAALHVARTVC 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767974050  98 RRAERRVVPLVQMGETDANVAKFLNRLSDYLFTLARYAAMKEGNQEKIY 146
Cdd:COG2096  128 RRAERRLVALAEEEPVNPEVLKYLNRLSDLLFVLARVANKRAGVAEVLW 176
PduO_Nterm TIGR00636
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin ...
 20-146 4.75e-42

ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin adenosyltransferase family corresponding to the N-terminal half of Salmonella PduO, a 1,2-propanediol utilization protein that probably is bifunctional. PduO represents one of at least three families of ATP:corrinoid adenosyltransferase: others are CobA (which partially complements PduO) and EutT. It was not clear originally whether ATP:cob(I)alamin adenosyltransferase activity resides in the N-terminal region of PduO, modeled here, but this has now become clear from the characterization of MeaD from Methylobacterium extorquens. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213544  Cd Length: 171  Bit Score: 137.85  E-value: 4.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974050   20 EELQKIQCTLQDVGSALATPCSSAR--EAHLKYttfkagpileLEQWIDKYTSQLPPLTAFILPSGGKISSALHFCRAVC 97
Cdd:TIGR00636  52 EDLERIQNDLFDIGGDLATPGDTKKitEEDVKW----------LEERIDQYRKELPPLKLFVLPGGTPAAAFLHVARTVA 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767974050   98 RRAERRVVPLVQMGETDANVAKFLNRLSDYLFTLARYAAMKEGNQEKIY 146
Cdd:TIGR00636 122 RRAERRVVALLKEEEINEVVLVYLNRLSDLLFVLARVVNKRSGVPEVIW 170
 
Name Accession Description Interval E-value
Cob_adeno_trans pfam01923
Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene ...
 5-135 3.45e-53

Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene products of PduO and EutT which are both cobalamin adenosyltransferases. PduO is a protein with ATP:cob(I)alamin adenosyltransferase activity. The main role of this protein is the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation.The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12.


Pssm-ID: 460384  Cd Length: 163  Bit Score: 165.75  E-value: 3.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974050    5 GFALELVTEkgHTFAEELQKIQCTLQDVGSALATPCSSAREahlkyTTFKAGPILELEQWIDKYTSQLPPLTAFILPSGG 84
Cdd:pfam01923  39 GLARALLPD--EDLRELLERIQNDLFDLGADLATPGPKEPK-----LRITEEDVERLEKEIDEYNAELPPLKSFILPGGS 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767974050   85 KISSALHFCRAVCRRAERRVVPLVQM-GETDANVAKFLNRLSDYLFTLARYA 135
Cdd:pfam01923 112 PAAAALHVARTVCRRAERRAVALAEEeEEAVRDVLKYLNRLSDLLFVLARYA 163
PduO COG2096
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin ...
 18-146 4.04e-51

Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441699  Cd Length: 180  Bit Score: 161.06  E-value: 4.04e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974050  18 FAEELQKIQCTLQDVGSALATPcsSAREAHLKYTtfkAGPILELEQWIDKYTSQLPPLTAFILPSGGKISSALHFCRAVC 97
Cdd:COG2096   53 LRELLERIQNDLFDLGADLATP--GEKRPPLRIT---EEDVERLEEEIDELNAELPPLKSFILPGGSPAAAALHVARTVC 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767974050  98 RRAERRVVPLVQMGETDANVAKFLNRLSDYLFTLARYAAMKEGNQEKIY 146
Cdd:COG2096  128 RRAERRLVALAEEEPVNPEVLKYLNRLSDLLFVLARVANKRAGVAEVLW 176
PduO_Nterm TIGR00636
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin ...
 20-146 4.75e-42

ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin adenosyltransferase family corresponding to the N-terminal half of Salmonella PduO, a 1,2-propanediol utilization protein that probably is bifunctional. PduO represents one of at least three families of ATP:corrinoid adenosyltransferase: others are CobA (which partially complements PduO) and EutT. It was not clear originally whether ATP:cob(I)alamin adenosyltransferase activity resides in the N-terminal region of PduO, modeled here, but this has now become clear from the characterization of MeaD from Methylobacterium extorquens. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213544  Cd Length: 171  Bit Score: 137.85  E-value: 4.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974050   20 EELQKIQCTLQDVGSALATPCSSAR--EAHLKYttfkagpileLEQWIDKYTSQLPPLTAFILPSGGKISSALHFCRAVC 97
Cdd:TIGR00636  52 EDLERIQNDLFDIGGDLATPGDTKKitEEDVKW----------LEERIDQYRKELPPLKLFVLPGGTPAAAFLHVARTVA 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767974050   98 RRAERRVVPLVQMGETDANVAKFLNRLSDYLFTLARYAAMKEGNQEKIY 146
Cdd:TIGR00636 122 RRAERRVVALLKEEEINEVVLVYLNRLSDLLFVLARVVNKRSGVPEVIW 170
 
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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