COBU_ECOLI
ID COBU_ECOLI Reviewed; 181 AA.
AC P0AE76; P46886;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Bifunctional adenosylcobalamin biosynthesis protein CobU;
DE AltName: Full=Adenosylcobinamide kinase;
DE EC=2.7.1.156 {ECO:0000250|UniProtKB:Q05599};
DE AltName: Full=Adenosylcobinamide-phosphate guanylyltransferase;
DE EC=2.7.7.62 {ECO:0000250|UniProtKB:Q05599};
GN Name=cobU; OrderedLocusNames=b1993, JW1971;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7592411; DOI=10.1128/jb.177.22.6371-6380.1995;
RA Lawrence J.G., Roth J.R.;
RT "The cobalamin (coenzyme B12) biosynthetic genes of Escherichia coli.";
RL J. Bacteriol. 177:6371-6380(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide
CC and addition of GMP to adenosylcobinamide phosphate.
CC {ECO:0000250|UniProtKB:Q05599}.
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:0000250|UniProtKB:Q05599};
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:0000250|UniProtKB:Q05599};
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:0000250|UniProtKB:Q05599};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 6/7.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: By cobinamide.
CC -!- SIMILARITY: Belongs to the CobU/CobP family. {ECO:0000305}.
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DR EMBL; U33333; AAA78906.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75054.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15810.1; -; Genomic_DNA.
DR PIR; H64963; H64963.
DR RefSeq; NP_416497.1; NC_000913.3.
DR RefSeq; WP_000973176.1; NZ_SSUV01000031.1.
DR AlphaFoldDB; P0AE76; -.
DR SMR; P0AE76; -.
DR BioGRID; 4262116; 22.
DR IntAct; P0AE76; 4.
DR STRING; 511145.b1993; -.
DR jPOST; P0AE76; -.
DR PaxDb; P0AE76; -.
DR PRIDE; P0AE76; -.
DR EnsemblBacteria; AAC75054; AAC75054; b1993.
DR EnsemblBacteria; BAA15810; BAA15810; BAA15810.
DR GeneID; 66674118; -.
DR GeneID; 946519; -.
DR KEGG; ecj:JW1971; -.
DR KEGG; eco:b1993; -.
DR PATRIC; fig|511145.12.peg.2068; -.
DR EchoBASE; EB3027; -.
DR eggNOG; COG2087; Bacteria.
DR HOGENOM; CLU_094161_0_2_6; -.
DR InParanoid; P0AE76; -.
DR OMA; DCLTVWL; -.
DR PhylomeDB; P0AE76; -.
DR BioCyc; EcoCyc:COBU-MON; -.
DR UniPathway; UPA00148; UER00236.
DR UniPathway; UPA00148; UER00237.
DR PRO; PR:P0AE76; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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-KW.
DR GO; GO:0008819; F:cobinamide kinase activity; ISS:EcoCyc.
DR GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; ISS:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00544; CobU; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Cobalamin biosynthesis; GTP-binding; Kinase;
KW Nucleotide-binding; Porphyrin biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..181
FT /note="Bifunctional adenosylcobalamin biosynthesis protein
FT CobU"
FT /id="PRO_0000089996"
FT ACT_SITE 47
FT /note="GMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 7..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 31..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 48..51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 181 AA; 20164 MW; 072EB233416EBCB1 CRC64;
MMILVTGGAR SGKSRHAEAL IGDSSQVLYI ATSQILDDEM AARIEHHRQG RPEHWRTVER
WQHLDELIHA DINPNEVVLL ECVTTMVTNL LFDYGGDKDP DEWDYQAMEQ AINAEIQSLI
AACQRCPAKV VLVTNEVGMG IVPESRLARH FRDIAGRVNQ QLAAAANEVW LVVSGIGVKI
K
