COBU_ECO57
ID COBU_ECO57 Reviewed; 181 AA.
AC P0AE77; P46886;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Z3153, ECs2788;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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. {ECO:0000250|UniProtKB:Q05599}.
CC -!- SIMILARITY: Belongs to the CobU/CobP family. {ECO:0000305}.
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DR EMBL; AE005174; AAG57054.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36211.1; -; Genomic_DNA.
DR PIR; B85824; B85824.
DR PIR; D90977; D90977.
DR RefSeq; NP_310815.1; NC_002695.1.
DR RefSeq; WP_000973176.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AE77; -.
DR SMR; P0AE77; -.
DR STRING; 155864.EDL933_3064; -.
DR EnsemblBacteria; AAG57054; AAG57054; Z3153.
DR EnsemblBacteria; BAB36211; BAB36211; ECs_2788.
DR GeneID; 66674118; -.
DR GeneID; 912633; -.
DR KEGG; ece:Z3153; -.
DR KEGG; ecs:ECs_2788; -.
DR PATRIC; fig|386585.9.peg.2921; -.
DR eggNOG; COG2087; Bacteria.
DR HOGENOM; CLU_094161_0_2_6; -.
DR OMA; DCLTVWL; -.
DR UniPathway; UPA00148; UER00236.
DR UniPathway; UPA00148; UER00237.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0008820; F:cobinamide phosphate guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
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_0000089997"
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
