ID   PDUO_CITFR              Reviewed;         335 AA.
AC   B1VB74;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Corrinoid adenosyltransferase PduO;
DE   AltName: Full=ATP:co(I)rrinoid adenosyltransferase PduO;
DE            Short=ACA;
DE   AltName: Full=Propanediol utilization protein PduO;
GN   Name=pduO {ECO:0000303|PubMed:18332146};
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], FUNCTION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, PATHWAY, AND SUBCELLULAR LOCATION.
RX   PubMed=18332146; DOI=10.1074/jbc.m709214200;
RA   Parsons J.B., Dinesh S.D., Deery E., Leech H.K., Brindley A.A., Heldt D.,
RA   Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., Bleloch A.,
RA   McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., Prentice M.B.;
RT   "Biochemical and Structural Insights into Bacterial Organelle Form and
RT   Biogenesis.";
RL   J. Biol. Chem. 283:14366-14375(2008).
CC   -!- FUNCTION: Converts cob(I)alamin to adenosylcobalamin
CC       (adenosylcob(III)alamin), the cofactor for propanediol dehydratase.
CC       Found in the bacterial microcompartment (BMC) dedicated to 1,2-
CC       propanediol (1,2-PD) degradation. PduS and PduO allow regeneration of
CC       the adenosylcobalamin cofactor within the BMC.
CC       {ECO:0000250|UniProtKB:Q8ZNR5}.
CC   -!- FUNCTION: Expression of a cosmid containing the full 21-gene pdu operon
CC       in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the
CC       appearance of bacterial microcompartments (BMC) in its cytoplasm.
CC       {ECO:0000269|PubMed:18332146}.
CC   -!- FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC)
CC       concentrates low levels of 1,2-PD catabolic enzymes, concentrates
CC       volatile reaction intermediates thus enhancing pathway flux and keeps
CC       the level of toxic, mutagenic propionaldehyde low.
CC       {ECO:0000305|PubMed:18332146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cob(I)alamin-[corrinoid adenosyltransferase] =
CC         adenosylcob(III)alamin + apo-[corrinoid adenosyltransferase] +
CC         triphosphate; Xref=Rhea:RHEA:56796, Rhea:RHEA-COMP:14743, Rhea:RHEA-
CC         COMP:14744, ChEBI:CHEBI:18036, ChEBI:CHEBI:18408, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:60488, ChEBI:CHEBI:83228;
CC         Evidence={ECO:0000250|UniProtKB:Q8ZNR5};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:Q8ZNR5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8ZNR5};
CC   -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC       {ECO:0000269|PubMed:18332146}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Forms a complex with PduS. {ECO:0000250|UniProtKB:Q8ZNR5}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000269|PubMed:18332146}.
CC   -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC       PduO subfamily. {ECO:0000305}.
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DR   EMBL; AM498294; CAM57295.1; -; Genomic_DNA.
DR   UniPathway; UPA00148; -.
DR   UniPathway; UPA00621; -.
DR   GO; GO:0031469; C:bacterial microcompartment; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.1200.10; -; 1.
DR   Gene3D; 3.30.450.150; -; 1.
DR   InterPro; IPR016030; CblAdoTrfase-like.
DR   InterPro; IPR036451; CblAdoTrfase-like_sf.
DR   InterPro; IPR009221; PduO.
DR   InterPro; IPR029499; PduO-typ.
DR   InterPro; IPR005624; PduO/GlcC-like.
DR   InterPro; IPR038084; PduO/GlcC-like_sf.
DR   PANTHER; PTHR12213; PTHR12213; 1.
DR   Pfam; PF01923; Cob_adeno_trans; 1.
DR   Pfam; PF03928; Haem_degrading; 1.
DR   PIRSF; PIRSF036411; ATR_PduO; 1.
DR   SUPFAM; SSF143744; SSF143744; 1.
DR   SUPFAM; SSF89028; SSF89028; 1.
DR   TIGRFAMs; TIGR00636; PduO_Nterm; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Bacterial microcompartment; Cobalamin biosynthesis; Heme;
KW   Iron; Magnesium; Metal-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..335
FT                   /note="Corrinoid adenosyltransferase PduO"
FT                   /id="PRO_0000454281"
FT   BINDING         206
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZNR5"
SQ   SEQUENCE   335 AA;  36699 MW;  9853FDF3C0F7923B CRC64;
     MAIYTRTGDA GTTALFTGQR VSKTHPRVEA YGTLDELNAA LSLCVCAAKN PQHRQLLENI
     QLQLFWFSAE LASESEQPAP EQRYISSEEI AALEAAIDTA MGRVPPLRSF ILPGRSEAAS
     RLHFARTLAR RAERRLVELS TEISVRHVLM RYINRLSDCL YALARAEDHD AHQNNIIQKV
     AERYLAAIRT SATREPAMSL SFQELHQLTR AAVMRAEELQ VPVVISIVDA NGTQTVTWRM
     PDALLVSSEL APKKAWTAVA MKTATHELTS AVQPGAALYG LESHMQGKVV TFGGGYALWR
     EGLLLGGLGI SGGSVEQDMD IAETAIAAIN VRTHQ