(data stored in SCRATCH zone)

SWISSPROT: Q5LWD7_RUEPO

ID   Q5LWD7_RUEPO            Unreviewed;       174 AA.
AC   Q5LWD7;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Bifunctional adenosylcobalamin biosynthesis protein {ECO:0000256|PIRNR:PIRNR006135};
DE            EC=2.7.1.156 {ECO:0000256|PIRNR:PIRNR006135};
DE            EC=2.7.7.62 {ECO:0000256|PIRNR:PIRNR006135};
GN   OrderedLocusNames=SPO0405 {ECO:0000313|EMBL:AAV93723.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93723.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93723.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93723.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of
CC       adenosylcobinamide and addition of GMP to adenosylcobinamide
CC       phosphate. {ECO:0000256|PIRNR:PIRNR006135}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)inamide + ATP = adenosylcob(III)inamide
CC         phosphate + ADP + H(+); Xref=Rhea:RHEA:15769, ChEBI:CHEBI:2480,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58502,
CC         ChEBI:CHEBI:456216; EC=2.7.1.156;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006135};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)inamide phosphate + GTP + H(+) =
CC         adenosylcob(III)inamide-GDP + diphosphate; Xref=Rhea:RHEA:22712,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58502, ChEBI:CHEBI:60487; EC=2.7.7.62;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006135};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
CC       {ECO:0000256|PIRNR:PIRNR006135}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       adenosylcobalamin from cob(II)yrinate a,c-diamide: step 6/7.
CC       {ECO:0000256|PIRNR:PIRNR006135}.
CC   -!- SIMILARITY: Belongs to the CobU/CobP family.
CC       {ECO:0000256|PIRNR:PIRNR006135}.
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DR   EMBL; CP000031; AAV93723.1; -; Genomic_DNA.
DR   RefSeq; WP_011046166.1; NC_003911.12.
DR   STRING; 246200.SPO0405; -.
DR   EnsemblBacteria; AAV93723; AAV93723; SPO0405.
DR   KEGG; sil:SPO0405; -.
DR   eggNOG; ENOG4108YZT; Bacteria.
DR   eggNOG; COG2087; LUCA.
DR   HOGENOM; HOG000286613; -.
DR   KO; K02231; -.
DR   OMA; DCLTVWL; -.
DR   OrthoDB; 1903913at2; -.
DR   BioCyc; RPOM246200:G1G48-412-MONOMER; -.
DR   UniPathway; UPA00148; UER00236.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0043752; F:adenosylcobinamide kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR003203; Cobinamide_kinase/P_G-Trfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR34848; PTHR34848; 1.
DR   Pfam; PF02283; CobU; 1.
DR   PIRSF; PIRSF006135; CobU; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWD7.
DR   SWISS-2DPAGE; Q5LWD7.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR006135};
KW   Cobalamin biosynthesis {ECO:0000256|PIRNR:PIRNR006135};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   GTP-binding {ECO:0000256|PIRNR:PIRNR006135,
KW   ECO:0000256|PIRSR:PIRSR006135-2};
KW   Kinase {ECO:0000256|PIRNR:PIRNR006135, ECO:0000313|EMBL:AAV93723.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006135,
KW   ECO:0000256|PIRSR:PIRSR006135-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transferase {ECO:0000256|PIRNR:PIRNR006135,
KW   ECO:0000313|EMBL:AAV93723.1}.
FT   NP_BIND      11     18       GTP. {ECO:0000256|PIRSR:PIRSR006135-2}.
FT   NP_BIND      36     38       GTP. {ECO:0000256|PIRSR:PIRSR006135-2}.
FT   ACT_SITE     52     52       GMP-histidine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR006135-1}.
FT   BINDING      64     64       GTP. {ECO:0000256|PIRSR:PIRSR006135-2}.
FT   BINDING      85     85       GTP; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR006135-2}.
SQ   SEQUENCE   174 AA;  18681 MW;  E81C5B6A7448B330 CRC64;
     MLYPKFTLVL GGAASGKSSF AEQMVVSTGK SRVYFASSQV FDAEMQAKID RHLVQRGPGW
     TTIEEPLEPG PALSALSARD ICLFDCATMW LSNHLLAEGD LDAAQERLMA AIRHCPAQLV
     MVSNEVGHGI VPENALARRF REAQGRLNIA LAAEADLVVL VVAGLPLALK GQLP
//

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