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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down 12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down 12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down 12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down 12/28 - 12/31
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MetaCyc Enzyme: γ-butyrobetainyl-CoA:carnitine CoA transferase

Gene: caiB Accession Numbers: EG11559 (MetaCyc), b0038, ECK0039

Synonyms: yaaN

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of γ-butyrobetainyl-CoA:carnitine CoA transferase = [CaiB]2
         CaiB monomer = CaiB

Summary:
The crystal structure of CaiB has been solved and shows that two monomers form an interlaced dimer [Stenmark04].

CaiB was thought to be a carnitine dehydratase ([Jung89, Eichler94a]), but was later shown to be a type III CoA transferase [Elssner01]. The purified CaiB likely contained small amounts of CaiD, accounting for the observed activity [Elssner01].

In E. coli strain O44 K74, the caiB gene product forms a complex with the caiA gene product, crotonobetaine reductase. [Preusser99]

Locations: cytosol

Map Position: [37,898 <- 39,115]

Molecular Weight of Polypeptide: 45.127 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000136 , CGSC:36800 , EchoBASE:EB1520 , EcoGene:EG11559 , EcoliWiki:b0038 , ModBase:P31572 , OU-Microarray:b0038 , PortEco:caiB , PR:PRO_000022242 , Pride:P31572 , Protein Model Portal:P31572 , RefSeq:NP_414580 , RegulonDB:EG11559 , SMR:P31572 , String:511145.b0038 , UniProt:P31572

Relationship Links: InterPro:IN-FAMILY:IPR003673 , InterPro:IN-FAMILY:IPR023452 , InterPro:IN-FAMILY:IPR023606 , Panther:IN-FAMILY:PTHR11837 , PDB:Structure:1XA3 , PDB:Structure:1XA4 , PDB:Structure:1XK6 , PDB:Structure:1XK7 , PDB:Structure:1XVT , PDB:Structure:1XVU , PDB:Structure:1XVV , Pfam:IN-FAMILY:PF02515

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0042413 - carnitine catabolic process Inferred from experiment [Eichler94a]
GO:0009437 - carnitine metabolic process Inferred by computational analysis [UniProtGOA12, GOA01a]
Molecular Function: GO:0008735 - carnitine dehydratase activity Inferred from experiment [Eichler94a, Eichler94]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0008410 - CoA-transferase activity Inferred by computational analysis [GOA06]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016782 - transferase activity, transferring sulfur-containing groups Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism central intermediary metabolism carnitine metabolism

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: γ-butyrobetainyl-CoA:carnitine CoA transferase

γ-butyrobetainyl-CoA + L-carnitine <=> γ-butyrobetaine + L-carnitinyl-CoA

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: L-carnitine degradation I

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Sequence Features

Feature Class Location Citations Comment
Amino-Acid-Sites-That-Bind 97
[UniProt10]
UniProt: Coenzyme A;
Amino-Acid-Sites-That-Bind 104
[UniProt10]
UniProt: Coenzyme A;
Active-Site 169
[UniProt10]
UniProt: Nucleophile;
Extrinsic-Sequence-Variant 187
[UniProt10]
Alternate sequence: A; UniProt: (in strain: O44:K74);
Extrinsic-Sequence-Variant 302
[UniProt10]
Alternate sequence: A; UniProt: (in strain: O44:K74);

History:
10/20/97 Gene b0038 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11559; confirmed by SwissProt match.


References

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

Eichler94: Eichler K, Bourgis F, Buchet A, Kleber HP, Mandrand-Berthelot MA (1994). "Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli." Mol Microbiol 1994;13(5);775-86. PMID: 7815937

Eichler94a: Eichler K, Schunck WH, Kleber HP, Mandrand-Berthelot MA (1994). "Cloning, nucleotide sequence, and expression of the Escherichia coli gene encoding carnitine dehydratase." J Bacteriol 1994;176(10);2970-5. PMID: 8188598

Elssner01: Elssner T, Engemann C, Baumgart K, Kleber HP (2001). "Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli." Biochemistry 40(37);11140-8. PMID: 11551212

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Jung89: Jung H, Jung K, Kleber HP (1989). "Purification and properties of carnitine dehydratase from Escherichia coli--a new enzyme of carnitine metabolization." Biochim Biophys Acta 1989;1003(3);270-6. PMID: 2663076

Preusser99: Preusser A, Wagner U, Elssner T, Kleber HP (1999). "Crotonobetaine reductase from Escherichia coli consists of two proteins." Biochim Biophys Acta 1999;1431(1);166-78. PMID: 10209289

Stenmark04: Stenmark P, Gurmu D, Nordlund P (2004). "Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism." Biochemistry 43(44);13996-4003. PMID: 15518548

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

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

UniProtGOA11a: 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 MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, BIOCYC14A.