COBO_PSEAE
ID COBO_PSEAE Reviewed; 203 AA.
AC Q9I472;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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;
GN Name=cobO; OrderedLocusNames=PA1272;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Required for both de novo synthesis of the corrin ring for
CC the assimilation of exogenous corrinoids. Participates in the
CC adenosylation of a variety of incomplete and complete corrinoids (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG04661.1; -; Genomic_DNA.
DR PIR; F83485; F83485.
DR RefSeq; NP_249963.1; NC_002516.2.
DR RefSeq; WP_003086769.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I472; -.
DR SMR; Q9I472; -.
DR STRING; 287.DR97_663; -.
DR PaxDb; Q9I472; -.
DR PRIDE; Q9I472; -.
DR EnsemblBacteria; AAG04661; AAG04661; PA1272.
DR GeneID; 881408; -.
DR KEGG; pae:PA1272; -.
DR PATRIC; fig|208964.12.peg.1322; -.
DR PseudoCAP; PA1272; -.
DR HOGENOM; CLU_088595_0_0_6; -.
DR InParanoid; Q9I472; -.
DR OMA; VVKHAFK; -.
DR PhylomeDB; Q9I472; -.
DR BioCyc; PAER208964:G1FZ6-1297-MON; -.
DR UniPathway; UPA00148; UER00233.
DR Proteomes; UP000002438; Chromosome.
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 CDD; cd00561; CobA_CobO_BtuR; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003724; CblAdoTrfase_CobA.
DR InterPro; IPR025826; Co_AT_N_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF12557; Co_AT_N; 1.
DR Pfam; PF02572; CobA_CobO_BtuR; 1.
DR PIRSF; PIRSF015617; Adensltrnsf_CobA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00708; cobA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cobalamin biosynthesis; Cytoplasm; Manganese;
KW Nucleotide-binding; Porphyrin biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..203
FT /note="Corrinoid adenosyltransferase"
FT /id="PRO_0000287788"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 203 AA; 22292 MW; 2176356693732743 CRC64;
MNESPEKDQR HRERMERKKA VVDEKIAQAR DERGVLLVHS GNGKGKSSSA FGMVARALGH
GMKVGVVQFI KGAASTGEEA FFRRFPEEVS YHVMGEGFTW ETQDRQRDIA KAEAAWKVAA
QLLADPDVGL VVLDELNIAL KHGYLELDRV LADIQARPAM QHVVVTGRGA QPGMIEAADT
VTEMSLVKHA FKAGIKAQKG VEF
