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Bifunctional adenosylcobalamin biosynthesis protein (EC 2.7.1.156) (EC 2.7.7.62)

 A0A166B112_9RHOB        Unreviewed;       187 AA.
A0A166B112;
06-JUL-2016, integrated into UniProtKB/TrEMBL.
06-JUL-2016, sequence version 1.
05-DEC-2018, entry version 13.
RecName: Full=Bifunctional adenosylcobalamin biosynthesis protein {ECO:0000256|PIRNR:PIRNR006135};
EC=2.7.1.156 {ECO:0000256|PIRNR:PIRNR006135};
EC=2.7.7.62 {ECO:0000256|PIRNR:PIRNR006135};
Name=cobP {ECO:0000313|EMBL:KZL21802.1};
ORFNames=PsAD2_00227 {ECO:0000313|EMBL:KZL21802.1};
Pseudovibrio axinellae.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Pseudovibrio.
NCBI_TaxID=989403 {ECO:0000313|EMBL:KZL21802.1, ECO:0000313|Proteomes:UP000076577};
[1] {ECO:0000313|EMBL:KZL21802.1, ECO:0000313|Proteomes:UP000076577}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ad2 {ECO:0000313|EMBL:KZL21802.1,
ECO:0000313|Proteomes:UP000076577};
PubMed=27065959; DOI=10.3389/fmicb.2016.00387;
Romano S., Fernandez-Guerra A., Reen F.J., Glockner F.O.,
Crowley S.P., O'Sullivan O., Cotter P.D., Adams C., Dobson A.D.,
O'Gara F.;
"Comparative Genomic Analysis Reveals a Diverse Repertoire of Genes
Involved in Prokaryote-Eukaryote Interactions within the Pseudovibrio
Genus.";
Front. Microbiol. 7:387-387(2016).
-!- FUNCTION: Catalyzes ATP-dependent phosphorylation of
adenosylcobinamide and addition of GMP to adenosylcobinamide
phosphate. {ECO:0000256|PIRNR:PIRNR006135}.
-!- CATALYTIC ACTIVITY:
Reaction=adenosylcob(III)inamide + ATP = adenosylcob(III)inamide
phosphate + ADP + H(+); Xref=Rhea:RHEA:15769, ChEBI:CHEBI:2480,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58502,
ChEBI:CHEBI:456216; EC=2.7.1.156;
Evidence={ECO:0000256|PIRNR:PIRNR006135};
-!- CATALYTIC ACTIVITY:
Reaction=adenosylcob(III)inamide phosphate + GTP + H(+) =
adenosylcob(III)inamide-GDP + diphosphate; Xref=Rhea:RHEA:22712,
ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
ChEBI:CHEBI:58502, ChEBI:CHEBI:60487; EC=2.7.7.62;
Evidence={ECO:0000256|PIRNR:PIRNR006135};
-!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
{ECO:0000256|PIRNR:PIRNR006135}.
-!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
adenosylcobalamin from cob(II)yrinate a,c-diamide: step 6/7.
{ECO:0000256|PIRNR:PIRNR006135}.
-!- SIMILARITY: Belongs to the CobU/CobP family.
{ECO:0000256|PIRNR:PIRNR006135}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KZL21802.1}.
-----------------------------------------------------------------------
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EMBL; LMCB01000002; KZL21802.1; -; Genomic_DNA.
EnsemblBacteria; KZL21802; KZL21802; PsAD2_00227.
PATRIC; fig|989403.3.peg.238; -.
UniPathway; UPA00148; UER00236.
UniPathway; UPA00148; UER00237.
Proteomes; UP000076577; Unassembled WGS sequence.
GO; GO:0043752; F:adenosylcobinamide kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd00544; CobU; 1.
InterPro; IPR003203; Cobinamide_kinase/P_G-Trfase.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR34848; PTHR34848; 1.
Pfam; PF02283; CobU; 1.
PIRSF; PIRSF006135; CobU; 1.
SUPFAM; SSF52540; SSF52540; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|PIRNR:PIRNR006135};
Cobalamin biosynthesis {ECO:0000256|PIRNR:PIRNR006135};
Complete proteome {ECO:0000313|Proteomes:UP000076577};
GTP-binding {ECO:0000256|PIRNR:PIRNR006135,
ECO:0000256|PIRSR:PIRSR006135-2};
Kinase {ECO:0000256|PIRNR:PIRNR006135};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006135,
ECO:0000256|PIRSR:PIRSR006135-2};
Reference proteome {ECO:0000313|Proteomes:UP000076577};
Transferase {ECO:0000256|PIRNR:PIRNR006135}.
NP_BIND 18 25 GTP. {ECO:0000256|PIRSR:PIRSR006135-2}.
NP_BIND 43 45 GTP. {ECO:0000256|PIRSR:PIRSR006135-2}.
ACT_SITE 59 59 GMP-histidine intermediate.
{ECO:0000256|PIRSR:PIRSR006135-1}.
BINDING 71 71 GTP. {ECO:0000256|PIRSR:PIRSR006135-2}.
BINDING 93 93 GTP; via carbonyl oxygen.
{ECO:0000256|PIRSR:PIRSR006135-2}.
SEQUENCE 187 AA; 20961 MW; 89A81EAF11A6406B CRC64;
MMAEHSKDLC TRHCLVTGGA RSGKSAYAEK LVLRSGRRAT YIATGQAFDL EMEERITLHQ
TQRGSDWDTI EEPLELVSAL ERCAGAERAI LVDCLTLWLS NLMHAERDWT RELEKLQLVL
AQLRCPVVFV GNEVGMGIVP DNAMARAFRD EAGRLNQRIG ELCHFVMFVA AGQPLQLKPA
VHPEIYL


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