ID A0A4R0X8S2_9BURK Unreviewed; 200 AA.
AC A0A4R0X8S2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Corrinoid adenosyltransferase {ECO:0000256|ARBA:ARBA00012454, ECO:0000256|PIRNR:PIRNR015617};
DE EC=2.5.1.17 {ECO:0000256|ARBA:ARBA00012454, ECO:0000256|PIRNR:PIRNR015617};
DE AltName: Full=Cob(II)alamin adenosyltransferase {ECO:0000256|PIRNR:PIRNR015617};
DE AltName: Full=Cob(II)yrinic acid a,c-diamide adenosyltransferase {ECO:0000256|PIRNR:PIRNR015617};
GN ORFNames=BZM27_24720 {ECO:0000313|EMBL:TCG06656.1};
OS Paraburkholderia steynii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1245441 {ECO:0000313|EMBL:TCG06656.1, ECO:0000313|Proteomes:UP000294200};
RN [1] {ECO:0000313|EMBL:TCG06656.1, ECO:0000313|Proteomes:UP000294200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HC1.1ba {ECO:0000313|EMBL:TCG06656.1,
RC ECO:0000313|Proteomes:UP000294200};
RA Steenkamp E.T., Beukes C.W., Van Zyl E., Avontuur J., Chan W.Y., Hassen A.,
RA Palmer M., Mthombeni L., Phalane F., Sereme K., Venter S.N.;
RT "Paraburkholderia sophoroidis sp. nov. and Paraburkholderia steynii sp.
RT nov. rhizobial symbionts of the fynbos legume Hypocalyptus sophoroides.";
RL Submitted (FEB-2017) 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, ECO:0000256|PIRNR:PIRNR015617}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 cob(II)alamin + reduced [electron-transfer flavoprotein] + 2
CC ATP = 2 adenosylcob(III)alamin + 2 triphosphate + oxidized [electron-
CC transfer flavoprotein] + 3 H(+); Xref=Rhea:RHEA:28671, Rhea:RHEA-
CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16304, ChEBI:CHEBI:18036, ChEBI:CHEBI:18408,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=2.5.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00048692,
CC ECO:0000256|PIRNR:PIRNR015617};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 cob(II)yrinate a,c diamide + reduced [electron-transfer
CC flavoprotein] + 2 ATP = 2 adenosylcob(III)yrinate a,c-diamide + 2
CC triphosphate + oxidized [electron-transfer flavoprotein] + 3 H(+);
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:ARBA00048555,
CC ECO:0000256|PIRNR:PIRNR015617};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
CC {ECO:0000256|ARBA:ARBA00005121, ECO:0000256|PIRNR:PIRNR015617}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR015617}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007487, ECO:0000256|PIRNR:PIRNR015617}.
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:TCG06656.1}.
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DR EMBL; MWML01000097; TCG06656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R0X8S2; -.
DR UniPathway; UPA00148; UER00233.
DR Proteomes; UP000294200; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008817; F:corrinoid adenosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00708; cobA; 1.
DR NCBIfam; NF004637; PRK05986.1; 1.
DR PANTHER; PTHR46638; CORRINOID ADENOSYLTRANSFERASE; 1.
DR PANTHER; PTHR46638:SF1; CORRINOID ADENOSYLTRANSFERASE; 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 ATP-binding {ECO:0000256|PIRNR:PIRNR015617};
KW Cobalamin biosynthesis {ECO:0000256|PIRNR:PIRNR015617};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR015617};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR015617};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|PIRNR:PIRNR015617};
KW Reference proteome {ECO:0000313|Proteomes:UP000294200};
KW Transferase {ECO:0000256|PIRNR:PIRNR015617, ECO:0000313|EMBL:TCG06656.1}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 200 AA; 22410 MW; F1D6CCC55447A083 CRC64;
MKTDPESHAR MTQRRREGHE KKQAQATIEK GLLIVNTGTG KGKSTAAFGM AVRVLGHGMK
LGVVQFIKGA LHTSERDFLG AQANCDFVTM GDGYTWNTQD READMATARK GWNEARRMIE
SGEYQMVILD ELNTVLKYEY LPLEEVLDVV NARPEMLHVV ITGRHAPDAL IDAADLVTEM
RIVKHPYREQ HGESARGVEF
//
