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Database: UniProt
Entry: Q66AJ4_YERPS
LinkDB: Q66AJ4_YERPS
Original site: Q66AJ4_YERPS 
ID   Q66AJ4_YERPS            Unreviewed;       196 AA.
AC   Q66AJ4;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 95.
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   Name=btuR {ECO:0000313|EMBL:CAH21374.1};
GN   OrderedLocusNames=YPTB2136 {ECO:0000313|EMBL:CAH21374.1};
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH21374.1, ECO:0000313|Proteomes:UP000001011};
RN   [1] {ECO:0000313|EMBL:CAH21374.1, ECO:0000313|Proteomes:UP000001011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH21374.1; -; Genomic_DNA.
DR   RefSeq; WP_002210626.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66AJ4; -.
DR   GeneID; 66841432; -.
DR   KEGG; ypo:BZ17_328; -.
DR   KEGG; yps:YPTB2136; -.
DR   PATRIC; fig|273123.14.peg.347; -.
DR   OMA; HAMGEGF; -.
DR   UniPathway; UPA00148; UER00233.
DR   Proteomes; UP000001011; 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   Transferase {ECO:0000256|PIRNR:PIRNR015617, ECO:0000313|EMBL:CAH21374.1}.
FT   DOMAIN          3..21
FT                   /note="Cob(I)alamin adenosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12557"
SQ   SEQUENCE   196 AA;  21889 MW;  014B23086BA3CEDA CRC64;
     MSEDRHQQRQ QRLKEKVDSR IAAAQEVRGI LIVFTGNGKG KTTAAFGTVT RAVGHGLKAG
     VIQFIKGEWP NGEKNLLQQH GVEFQVMATG FTWNTQDRET DTVACLGVWQ HALRMLADPT
     LDLVVLDELT YMIAYDYLPL DEVINALNQR PAHQTVIITG RGCHRDLLEM ADTVSELRPV
     KHAFDAGIKA QQGIDW
//
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