ATR_CUPMC
ID ATR_CUPMC Reviewed; 184 AA.
AC Q1LJ80;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cobalamin adenosyltransferase {ECO:0000305|PubMed:28130442};
DE Short=ATR {ECO:0000303|PubMed:28130442};
DE EC=2.5.1.- {ECO:0000269|PubMed:28130442};
GN Name=cobO {ECO:0000312|EMBL:ABF09796.1};
GN OrderedLocusNames=Rmet_2923 {ECO:0000312|EMBL:ABF09796.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP GTP/GDP-BINDING, AND ACTIVITY REGULATION.
RX PubMed=28130442; DOI=10.1074/jbc.m117.775957;
RA Li Z., Kitanishi K., Twahir U.T., Cracan V., Chapman D., Warncke K.,
RA Banerjee R.;
RT "Cofactor editing by the G-protein metallochaperone domain regulates the
RT radical B12 enzyme IcmF.";
RL J. Biol. Chem. 292:3977-3987(2017).
CC -!- FUNCTION: Adenosyltransferase that catalyzes the conversion of
CC cob(II)alamin to adenosylcob(III)alamin (AdoCbl) in the presence of ATP
CC and an electron donor. Acts as an accessory protein of IcmF that
CC functions in cofactor repair, since IcmF is prone to inactivation
CC during catalytic turnover due to the occasional loss of the 5'-
CC deoxyadenosine moiety and formation of the inactive cob(II)alamin
CC cofactor in its active site. Thus, receives and repairs the inactive
CC cofactor, which is then reloaded onto IcmF in a GTPase-gated step.
CC {ECO:0000269|PubMed:28130442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + 2 ATP + 2 cob(II)alamin = A + 2 adenosylcob(III)alamin +
CC 2 H(+) + 2 triphosphate; Xref=Rhea:RHEA:53304, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16304, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:18036, ChEBI:CHEBI:18408, ChEBI:CHEBI:30616;
CC Evidence={ECO:0000269|PubMed:28130442};
CC -!- ACTIVITY REGULATION: Is potentially allosterically regulated by
CC GTP/GDP, which enhances its affinity for AdoCbl by 5-fold. Binds
CC cob(II)alamin weakly in the absence of ATP. The presence of ATP (but
CC not GTP or GDP) increases the affinity of cob(II)alamin for the enzyme,
CC and stoichiometric binding is observed. GTP blocks the transfer of
CC cob(II)alamin to IcmF from ATR, thus averting its reconstitution with
CC inactive cofactor. {ECO:0000269|PubMed:28130442}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 uM for ATP {ECO:0000269|PubMed:28130442};
CC Note=kcat is 3.8 min(-1). {ECO:0000269|PubMed:28130442};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:28130442}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CP000352; ABF09796.1; -; Genomic_DNA.
DR RefSeq; WP_011517468.1; NC_007973.1.
DR AlphaFoldDB; Q1LJ80; -.
DR SMR; Q1LJ80; -.
DR STRING; 266264.Rmet_2923; -.
DR PRIDE; Q1LJ80; -.
DR EnsemblBacteria; ABF09796; ABF09796; Rmet_2923.
DR GeneID; 60820641; -.
DR KEGG; rme:Rmet_2923; -.
DR eggNOG; COG2096; Bacteria.
DR HOGENOM; CLU_083486_0_1_4; -.
DR OMA; HQACTVV; -.
DR OrthoDB; 1401910at2; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:0030091; P:protein repair; IDA:UniProtKB.
DR Gene3D; 1.20.1200.10; -; 1.
DR InterPro; IPR016030; CblAdoTrfase-like.
DR InterPro; IPR036451; CblAdoTrfase-like_sf.
DR InterPro; IPR029499; PduO-typ.
DR PANTHER; PTHR12213; PTHR12213; 1.
DR Pfam; PF01923; Cob_adeno_trans; 1.
DR SUPFAM; SSF89028; SSF89028; 1.
DR TIGRFAMs; TIGR00636; PduO_Nterm; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cobalamin biosynthesis; GTP-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..184
FT /note="Cobalamin adenosyltransferase"
FT /id="PRO_0000439947"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT BINDING 18..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT BINDING 28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT BINDING 130..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
SQ SEQUENCE 184 AA; 19904 MW; 9C8C8EDF9340F3EB CRC64;
MGNRLSKIAT RTGDAGTTGL GDGSRVGKNS LRIVAIGDVD ELNSHIGLLL TEPDLPEDVR
AALLHIQHDL FDLGGELSIP GYTLLKAPQV AQLDDWLAHY NAALPRLAEF ILPGGSRPAA
QAHICRTVCR RAERALVELG AAEALNEAPR QYLNRLSDLL FVLARVLNRA GGGSDVLWQR
ERES
