ATR_CITFR
ID ATR_CITFR Reviewed; 176 AA.
AC P45515;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Corrinoid adenosyltransferase;
DE EC=2.5.1.17;
DE AltName: Full=Cob(II)alamin adenosyltransferase;
DE AltName: Full=Cob(II)yrinic acid a,c-diamide adenosyltransferase;
DE AltName: Full=Cobinamide/cobalamin adenosyltransferase;
DE AltName: Full=ORFW;
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK;
RA Daniel R., Gottschalk G.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-
CC transfer flavoprotein] = 2 adenosylcob(III)yrinate a,c-diamide + 3
CC H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate;
CC Xref=Rhea:RHEA:11528, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:58503,
CC ChEBI:CHEBI:58537; EC=2.5.1.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 cob(II)alamin + reduced [electron-transfer
CC flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized
CC [electron-transfer flavoprotein] + 2 triphosphate;
CC Xref=Rhea:RHEA:28671, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16304, ChEBI:CHEBI:18036,
CC ChEBI:CHEBI:18408, ChEBI:CHEBI:30616, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307; EC=2.5.1.17;
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U09771; AAB48846.1; -; Genomic_DNA.
DR AlphaFoldDB; P45515; -.
DR SMR; P45515; -.
DR UniPathway; UPA00148; UER00233.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Cobalamin biosynthesis; Cytoplasm; Nucleotide-binding;
KW Porphyrin biosynthesis; Transferase.
FT CHAIN 1..176
FT /note="Corrinoid adenosyltransferase"
FT /id="PRO_0000103801"
FT BINDING 6..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 131..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 176 AA; 19846 MW; AEB560DD05EF3EB5 CRC64;
MYRIYTRTGD NGTTALFGGS RIDKDDIRVE AYGTVDELIS QLGVCYASTR QAELRQELHA
MQKMLFVLGA ELASDQKGLT RLKQRIGEED IQALEQLIDR NMAQSGPLKE FVIPGKNLAS
AQLHVARTLT RRLERILIAM GRTLTLRDEA RRYINRLSDA LFSMARIEET TPDVCA
