ID A0A1H8V232_9PROT Unreviewed; 201 AA.
AC A0A1H8V232;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 25.
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=SAMN05216333_14410 {ECO:0000313|EMBL:SEP09552.1};
OS Nitrosomonas oligotropha.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=42354 {ECO:0000313|EMBL:SEP09552.1, ECO:0000313|Proteomes:UP000198814};
RN [1] {ECO:0000313|Proteomes:UP000198814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm76 {ECO:0000313|Proteomes:UP000198814};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FODO01000044; SEP09552.1; -; Genomic_DNA.
DR RefSeq; WP_090322496.1; NZ_FNOE01000045.1.
DR AlphaFoldDB; A0A1H8V232; -.
DR STRING; 42354.SAMN05216333_14410; -.
DR OrthoDB; 9810309at2; -.
DR UniPathway; UPA00148; UER00233.
DR Proteomes; UP000198814; 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; IPR025826; Co_AT_N_dom.
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; 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 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:UP000198814};
KW Transferase {ECO:0000256|PIRNR:PIRNR015617, ECO:0000313|EMBL:SEP09552.1}.
FT DOMAIN 1..25
FT /note="Cob(I)alamin adenosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12557"
SQ SEQUENCE 201 AA; 22463 MW; ED4D22ACFED64DDE CRC64;
MTDSGRAERY RTRMQRKKEV IDEAIARADR EQGLLLILTG NGKGKSSSAF GMMARALGHG
MRVGVAQFIK GRSDTGEEAF FRKQDQVVWH VLGEGFTWDT QNLERDTETA QRGWAVVQEM
LRDPSLDLIV LDELTYPLKF GWLDLTVVLN DLKNRPAMQH VVITGRGAPE ALCEAADTVT
EMTDVKHAYR AGVQAQKGID L
//
