ID A0A0D7F205_RHOPL Unreviewed; 179 AA.
AC A0A0D7F205;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=corrinoid adenosyltransferase {ECO:0000256|ARBA:ARBA00012454};
DE EC=2.5.1.17 {ECO:0000256|ARBA:ARBA00012454};
DE AltName: Full=Cob(II)alamin adenosyltransferase {ECO:0000256|ARBA:ARBA00031529};
DE AltName: Full=Cob(II)yrinic acid a,c-diamide adenosyltransferase {ECO:0000256|ARBA:ARBA00033354};
DE AltName: Full=Cobinamide/cobalamin adenosyltransferase {ECO:0000256|ARBA:ARBA00033334};
DE Flags: Fragment;
GN ORFNames=OO17_06025 {ECO:0000313|EMBL:KIZ46876.1};
OS Rhodopseudomonas palustris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ46876.1, ECO:0000313|Proteomes:UP000032515};
RN [1] {ECO:0000313|EMBL:KIZ46876.1, ECO:0000313|Proteomes:UP000032515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL398 {ECO:0000313|EMBL:KIZ46876.1,
RC ECO:0000313|Proteomes:UP000032515};
RA Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT isolated from estuarine surface water.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00024929}.
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 Evidence={ECO:0000256|ARBA:ARBA00001328};
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 Evidence={ECO:0000256|ARBA:ARBA00000143};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
CC {ECO:0000256|ARBA:ARBA00005121}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007487}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIZ46876.1}.
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DR EMBL; JXXE01000116; KIZ46876.1; -; Genomic_DNA.
DR RefSeq; WP_044407143.1; NZ_JXXE01000116.1.
DR AlphaFoldDB; A0A0D7F205; -.
DR OrthoDB; 9810309at2; -.
DR UniPathway; UPA00148; UER00233.
DR Proteomes; UP000032515; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008817; F:corrinoid 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_ACA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003724; CblAdoTrfase_CobA.
DR InterPro; IPR025826; Co_AT_N_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00708; cobA; 1.
DR PANTHER; PTHR46638; CORRINOID ADENOSYLTRANSFERASE; 1.
DR PANTHER; PTHR46638:SF1; CORRINOID ADENOSYLTRANSFERASE; 1.
DR Pfam; PF12557; Co_AT_N; 1.
DR Pfam; PF02572; CobA_CobO_BtuR; 1.
DR PIRSF; PIRSF015617; Adensltrnsf_CobA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Transferase {ECO:0000313|EMBL:KIZ46876.1}.
FT DOMAIN 4..27
FT /note="Cob(I)alamin adenosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12557"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 179
FT /evidence="ECO:0000313|EMBL:KIZ46876.1"
SQ SEQUENCE 179 AA; 20206 MW; 7FFF4C061A654F40 CRC64;
MTATDSDDNA RHAEKARKHK AARDKIMAGK TGEKGLLIVH TGTGKGKTSA ALGMVFRHIG
HEMPVGVVQF TKSPKWDTGE ARLLAKFPEL VTLHIMGEGF TWETQDRERD IAAATKGWER
AKELIRDDRH RMVLLDELNI VLRYDYLPLD EVLTFLRDEK PADKHVVITG RNAKPELIE
//
