(data stored in SCRATCH zone)

SWISSPROT: Q13DG6_RHOPS

ID   Q13DG6_RHOPS            Unreviewed;       208 AA.
AC   Q13DG6;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 71.
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=RPD_0635 {ECO:0000313|EMBL:ABE37873.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37873.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37873.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37873.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000283; ABE37873.1; -; Genomic_DNA.
DR   RefSeq; WP_011501060.1; NC_007958.1.
DR   STRING; 316057.RPD_0635; -.
DR   EnsemblBacteria; ABE37873; ABE37873; RPD_0635.
DR   KEGG; rpd:RPD_0635; -.
DR   eggNOG; ENOG41068B1; Bacteria.
DR   eggNOG; COG2109; LUCA.
DR   HOGENOM; HOG000260311; -.
DR   KO; K19221; -.
DR   OMA; HAMGEGF; -.
DR   OrthoDB; 1690483at2; -.
DR   BioCyc; RPAL316057:RPD_RS03255-MONOMER; -.
DR   UniPathway; UPA00148; UER00233.
DR   Proteomes; UP000001818; 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: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; Q13DG6.
DR   SWISS-2DPAGE; Q13DG6.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR015617};
KW   Cobalamin biosynthesis {ECO:0000256|PIRNR:PIRNR015617};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR015617};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR015617};
KW   Porphyrin biosynthesis {ECO:0000256|PIRNR:PIRNR015617};
KW   Transferase {ECO:0000256|PIRNR:PIRNR015617,
KW   ECO:0000313|EMBL:ABE37873.1}.
FT   COILED       15     35       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   208 AA;  23394 MW;  9518719A09792217 CRC64;
     MTDAAPDRDD NARHAEKAKK RKAAHDRKLE GMTDQKGLLI VHTGTGKGKT SAALGMVFRH
     IGHDMPVGVV HFTKSEKWNT GEAKLLAKFP ELVTLHIMGE GFTWETQDRE RDVAAARAGW
     ERAKALIRDD RHRMVLLDEL NIVLRYDYLP ISEVIDFLRD EKPADKHVVI TGRNANPALI
     EIADLVTEMT LVKHPFRSGV KAQKGVEF
//

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