ID B1M4K5_METRJ Unreviewed; 185 AA.
AC B1M4K5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=Mrad2831_1469 {ECO:0000313|EMBL:ACB23464.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB23464.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB23464.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide
CC and addition of GMP to adenosylcobinamide phosphate.
CC {ECO:0000256|ARBA:ARBA00003889, 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|ARBA:ARBA00000312,
CC ECO:0000256|PIRNR:PIRNR006135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosylcob(III)inamide + GTP = adenosylcob(III)inamide
CC phosphate + GDP + H(+); Xref=Rhea:RHEA:15765, ChEBI:CHEBI:2480,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58502; EC=2.7.1.156;
CC Evidence={ECO:0000256|ARBA:ARBA00001522};
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|ARBA:ARBA00000711,
CC 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|ARBA:ARBA00005159, 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|ARBA:ARBA00004692, ECO:0000256|PIRNR:PIRNR006135}.
CC -!- SIMILARITY: Belongs to the CobU/CobP family.
CC {ECO:0000256|ARBA:ARBA00007490, ECO:0000256|PIRNR:PIRNR006135}.
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DR EMBL; CP001001; ACB23464.1; -; Genomic_DNA.
DR AlphaFoldDB; B1M4K5; -.
DR STRING; 426355.Mrad2831_1469; -.
DR KEGG; mrd:Mrad2831_1469; -.
DR eggNOG; COG2087; Bacteria.
DR HOGENOM; CLU_094161_0_1_5; -.
DR UniPathway; UPA00148; UER00236.
DR Proteomes; UP000006589; Chromosome.
DR GO; GO:0036429; F:adenosylcobinamide kinase (ATP-specific) activity; IEA:RHEA.
DR GO; GO:0036428; F:adenosylcobinamide kinase (GTP-specific) activity; IEA:RHEA.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00544; CobU; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003203; CobU/CobP.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR34848; -; 1.
DR PANTHER; PTHR34848:SF1; BIFUNCTIONAL ADENOSYLCOBALAMIN BIOSYNTHESIS PROTEIN COBU; 1.
DR Pfam; PF02283; CobU; 1.
DR PIRSF; PIRSF006135; CobU; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR006135};
KW Cobalamin biosynthesis {ECO:0000256|PIRNR:PIRNR006135};
KW GTP-binding {ECO:0000256|PIRNR:PIRNR006135, ECO:0000256|PIRSR:PIRSR006135-
KW 2}; Kinase {ECO:0000256|PIRNR:PIRNR006135};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR006135};
KW Nucleotidyltransferase {ECO:0000313|EMBL:ACB23464.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006135}.
FT ACT_SITE 54
FT /note="GMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-1"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT BINDING 38..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT BINDING 55..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT BINDING 85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
SQ SEQUENCE 185 AA; 19505 MW; 0C2AE0295D0DEEB8 CRC64;
MPQPTPRMTL VLGGARSGKS AYAEGLIEAC PGPWLYLATA QAFDDEMVDR IAQHRARRGG
AWRTRDVPLA LPEAVAEAEG PVLVDCLTLW LTNLILAEAD VAQATARLLA ACADAPGPLV
LVGNEVGLGI VPDNALARRF RDAAGRLHQQ LAARADRVVL TVAGLPLLVK PQPPQTQVRP
TGASA
//
