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Escherichia coli K-12 substr. MG1655 Enzyme: cobinamide-P guanylyltransferase / cobinamide kinase



Gene: cobU Accession Numbers: EG13238 (EcoCyc), b1993, ECK1988

Regulation Summary Diagram: ?

Subunit composition of cobinamide-P guanylyltransferase / cobinamide kinase = [CobU]2

Summary:
E. coli K-12, as well as natural isolates, can synthesize cobalamin only when supplied with the intermediate cobinamide [Lawrence96]. cobU encodes a predicted bifunctional protein complex with cobinamide kinase and cobinamide-P guanylyltransferase activity [Lawrence95].

Expression of the cobUST operon is induced by cobinamide [Lawrence95].

Locations: cytosol

Map Position: [2,063,243 <- 2,063,788] (44.47 centisomes)
Length: 546 bp / 181 aa

Molecular Weight of Polypeptide: 20.164 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006616 , EchoBASE:EB3027 , EcoGene:EG13238 , EcoliWiki:b1993 , ModBase:P0AE76 , OU-Microarray:b1993 , PortEco:cobU , PR:PRO_000022315 , Protein Model Portal:P0AE76 , RefSeq:NP_416497 , RegulonDB:EG13238 , SMR:P0AE76 , String:511145.b1993 , Swiss-Model:P0AE76 , UniProt:P0AE76

Relationship Links: InterPro:IN-FAMILY:IPR003203 , InterPro:IN-FAMILY:IPR027417 , Pfam:IN-FAMILY:PF02283

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0009236 - cobalamin biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11, GOA01, Lawrence95]
GO:0006779 - porphyrin-containing compound biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11]
GO:0051188 - cofactor biosynthetic process Inferred by computational analysis [GOA01]
Molecular Function: GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11]
GO:0005525 - GTP binding Inferred by computational analysis [UniProtGOA11]
GO:0008819 - cobinamide kinase activity Inferred by computational analysis [Lawrence95]
GO:0008820 - cobinamide phosphate guanylyltransferase activity Inferred by computational analysis [GOA01a, Lawrence95]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0043752 - adenosylcobinamide kinase activity Inferred by computational analysis [GOA01a, GOA01]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism biosynthesis of building blocks cofactors, small molecule carriers cobalamin

Essentiality data for cobU knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 09-Jul-2007 by Keseler I , SRI International


Enzymatic reaction of: cobinamide-P guanylyltransferase

Synonyms: adenosylcobinamide-P guanylyltransferase

EC Number: 2.7.7.62

adenosyl-cobinamide phosphate + GTP + H+ <=> adenosylcobinamide-GDP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: adenosylcobalamin salvage from cobinamide I


Enzymatic reaction of: cobinamide kinase

Synonyms: adenosylcobinamide kinase

EC Number: 2.7.1.156

adenosylcobinamide + ATP <=> adenosyl-cobinamide phosphate + ADP + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: adenosylcobalamin salvage from cobinamide I


Sequence Features

Feature Class Location Citations Comment
Nucleotide-Phosphate-Binding-Region 7 -> 14
[UniProt10]
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 31 -> 33
[UniProt10]
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Active-Site 47
[UniProt10]
UniProt: GMP-histidine intermediate; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 48 -> 51
[UniProt10]
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 59
[UniProt10]
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 81
[UniProt10]
UniProt: GTP; via carbonyl oxygen; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b1993 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG13238; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Lawrence95: Lawrence JG, Roth JR (1995). "The cobalamin (coenzyme B12) biosynthetic genes of Escherichia coli." J Bacteriol 1995;177(22);6371-80. PMID: 7592411

Lawrence96: Lawrence JG, Roth JR (1996). "Evolution of coenzyme B12 synthesis among enteric bacteria: evidence for loss and reacquisition of a multigene complex." Genetics 142(1);11-24. PMID: 8770581

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, BIOCYC13B.