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Database: UniProt
Entry: L0KKQ1_MESAW
LinkDB: L0KKQ1_MESAW
Original site: L0KKQ1_MESAW 
ID   L0KKQ1_MESAW            Unreviewed;       204 AA.
AC   L0KKQ1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
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   OrderedLocusNames=Mesau_03596 {ECO:0000313|EMBL:AGB45957.1};
OS   Mesorhizobium australicum (strain HAMBI 3006 / LMG 24608 / WSM2073).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=754035 {ECO:0000313|EMBL:AGB45957.1, ECO:0000313|Proteomes:UP000010998};
RN   [1] {ECO:0000313|Proteomes:UP000010998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24608 / HAMBI 3006 / WSM2073
RC   {ECO:0000313|Proteomes:UP000010998};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Gu W., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Reeve W.G., Howieson J.G., Tiwari R.P.,
RA   O'Hara G.W., Atkins C.A., Ronson C.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium australicum WSM2073.";
RL   Submitted (FEB-2012) 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 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         ECO:0000256|PIRNR:PIRNR015617};
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         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; CP003358; AGB45957.1; -; Genomic_DNA.
DR   RefSeq; WP_015317376.1; NC_019973.1.
DR   AlphaFoldDB; L0KKQ1; -.
DR   STRING; 754035.Mesau_03596; -.
DR   KEGG; mam:Mesau_03596; -.
DR   eggNOG; COG2109; Bacteria.
DR   HOGENOM; CLU_088595_0_0_5; -.
DR   OMA; HAMGEGF; -.
DR   OrthoDB; 9810309at2; -.
DR   UniPathway; UPA00148; UER00233.
DR   Proteomes; UP000010998; Chromosome.
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   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:UP000010998};
KW   Transferase {ECO:0000256|PIRNR:PIRNR015617, ECO:0000313|EMBL:AGB45957.1}.
FT   DOMAIN          6..27
FT                   /note="Cob(I)alamin adenosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12557"
SQ   SEQUENCE   204 AA;  22252 MW;  9F74A95A0AB0D5B2 CRC64;
     MTDIDDKDEE RHRAKMAKRK AVQDAEVAGK TIEKGLLIVN TGPGKGKTTA AFGLALRMLG
     YGKRVGVVQF IKGKWHTGEK DAFAAFGDRV VWHAMGEGFT WETQDLKRDI AAAEAAWAKA
     LELIADPSIS LVVLDELNIA LRYDYLALDK VVAALKARRE GLHIVVTGRN AKPALVEAAD
     LVTEMGVTKH HFSTGVKAQQ GIEF
//
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