(data stored in ACNUC29543 zone)

SWISSPROT: B2JRJ7_PARP8

ID   B2JRJ7_PARP8            Unreviewed;       200 AA.
AC   B2JRJ7;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Corrinoid adenosyltransferase {ECO:0000256|PIRNR:PIRNR015617};
DE            EC=2.5.1.17 {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=Bphy_3156 {ECO:0000313|EMBL:ACC72324.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72324.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- FUNCTION: Required for both de novo synthesis of the corrin ring
CC       for the assimilation of exogenous corrinoids. Participates in the
CC       adenosylation of a variety of incomplete and complete corrinoids.
CC       {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-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16304,
CC         ChEBI:CHEBI:18036, ChEBI:CHEBI:18408, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=2.5.1.17;
CC         Evidence={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 +
CC         3 H(+) + oxidized [electron-transfer flavoprotein] + 2
CC         triphosphate; Xref=Rhea:RHEA:11528, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:18036,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:58503, ChEBI:CHEBI:58537; EC=2.5.1.17;
CC         Evidence={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|PIRNR:PIRNR015617}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR015617}.
CC   -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase
CC       family. {ECO:0000256|PIRNR:PIRNR015617}.
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DR   EMBL; CP001044; ACC72324.1; -; Genomic_DNA.
DR   RefSeq; WP_012402497.1; NC_010623.1.
DR   STRING; 391038.Bphy_3156; -.
DR   EnsemblBacteria; ACC72324; ACC72324; Bphy_3156.
DR   GeneID; 27742851; -.
DR   KEGG; bph:Bphy_3156; -.
DR   eggNOG; ENOG41068B1; Bacteria.
DR   eggNOG; COG2109; LUCA.
DR   HOGENOM; HOG000260311; -.
DR   KO; K19221; -.
DR   OMA; HAMGEGF; -.
DR   OrthoDB; 1690483at2; -.
DR   BioCyc; BPHY391038:G1GBS-3254-MONOMER; -.
DR   UniPathway; UPA00148; UER00233.
DR   Proteomes; UP000001192; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide 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_CobO_BtuR; 1.
DR   InterPro; IPR003724; CblAdoTrfase_CobA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02572; CobA_CobO_BtuR; 1.
DR   PIRSF; PIRSF015617; Adensltrnsf_CobA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00708; cobA; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2JRJ7.
DR   SWISS-2DPAGE; B2JRJ7.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR015617};
KW   Cobalamin biosynthesis {ECO:0000256|PIRNR:PIRNR015617};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR015617};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR015617};
KW   Porphyrin biosynthesis {ECO:0000256|PIRNR:PIRNR015617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW   Transferase {ECO:0000256|PIRNR:PIRNR015617,
KW   ECO:0000313|EMBL:ACC72324.1}.
SQ   SEQUENCE   200 AA;  22509 MW;  109DCEDBD7AAE1EA CRC64;
     MKTDPESHAR MTQRRREGHE KKQAQATIEK GLLIVYTGTG KGKSTAAFGM AVRVLGHGLK
     LGVVQFIKGA LHTSERDFLG TQANCDFVTM GDGYTWNTQD READMATARK GWNEARRMIE
     SGEYQMVILD ELNTVLKYEY LPLEEVLGVI NARPEMLHVV ITGRHAPDAL IDAADLVTEM
     RLVKHPYREQ HVKAQRGVEF
//

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