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P31572 (CAIB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-carnitine CoA-transferase

EC=2.8.3.21
Alternative name(s):
Crotonobetainyl-CoA:carnitine CoA-transferase
Gene names
Name:caiB
Synonyms:yaaN
Ordered Locus Names:b0038, JW0037
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA. Ref.6

Catalytic activity

(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA. Ref.6 Ref.7

4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA. Ref.6 Ref.7

Pathway

Amine and polyamine metabolism; carnitine metabolism. HAMAP-Rule MF_01050

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_01050.

Induction

By L-carnitine or crotonobetaine. HAMAP-Rule MF_01050

Miscellaneous

Some strains of E.coli, such as ATCC 25922, can metabolize carnitine under aerobiosis.

Sequence similarities

Belongs to the CaiB/BaiF CoA-transferase family.

Caution

Was originally (Ref.1) thought to be an L-carnitine dehydratase.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarnitine catabolic process

Inferred from experiment Ref.1. Source: EcoliWiki

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionCoA-transferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

carnitine dehydratase activity

Inferred from experiment Ref.2Ref.1. Source: EcoliWiki

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405L-carnitine CoA-transferase HAMAP-Rule MF_01050
PRO_0000194708

Sites

Active site1691Nucleophile
Binding site971Coenzyme A
Binding site1041Coenzyme A

Natural variations

Natural variant1871V → A in strain: O44:K74.
Natural variant3021T → A in strain: O44:K74.

Secondary structure

.................................................................................... 405
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31572 [UniParc].

Last modified February 1, 1995. Version 3.
Checksum: 75583684B4B5A2DE

FASTA40545,127
        10         20         30         40         50         60 
MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ 

        70         80         90        100        110        120 
LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWQHNPKLVI 

       130        140        150        160        170        180 
AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGLTATTAA 

       190        200        210        220        230        240 
LAALHKVRET GKGESIDIAM YEVMLRMGQY FMMDYFNGGE MCPRMSKGKD PYYAGCGLYK 

       250        260        270        280        290        300 
CADGYIVMEL VGITQIEECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL 

       310        320        330        340        350        360 
ATHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF 

       370        380        390        400 
KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, nucleotide sequence, and expression of the Escherichia coli gene encoding carnitine dehydratase."
Eichler K., Schunck W.-H., Kleber H.-P., Mandrand-Berthelot M.-A.
J. Bacteriol. 176:2970-2975(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19.
Strain: O44:K74.
[2]"Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli."
Eichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A.
Mol. Microbiol. 13:775-786(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O44:K74.
[3]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"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."
Elssner T., Engemann C., Baumgart K., Kleber H.-P.
Biochemistry 40:11140-11148(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
Strain: O44:K74.
[7]"Metabolism of L(-)-carnitine by Enterobacteriaceae under aerobic conditions."
Elssner T., Preusser A., Wagner U., Kleber H.-P.
FEMS Microbiol. Lett. 174:295-301(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY UNDER AEROBIOSIS.
Strain: ATCC 25922 / DSM 1103 / NCIB 12210 and O44:K74.
[8]"Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism."
Stenmark P., Gurmu D., Nordlund P.
Biochemistry 43:13996-14003(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH COENZYME A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67748 Genomic DNA. Translation: CAA47971.1.
X73904 Genomic DNA. Translation: CAA52112.1.
U00096 Genomic DNA. Translation: AAC73149.1.
AP009048 Genomic DNA. Translation: BAB96607.1.
PIRS40559.
RefSeqNP_414580.1. NC_000913.3.
YP_488344.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XA3X-ray1.85A/B2-405[»]
1XA4X-ray1.90A/B2-405[»]
1XK6X-ray1.85A/B/C/D1-405[»]
1XK7X-ray1.60A/B/C1-405[»]
1XVTX-ray2.30A1-405[»]
1XVUX-ray2.40A1-405[»]
1XVVX-ray2.40A1-405[»]
ProteinModelPortalP31572.
SMRP31572. Positions 1-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP31572. 12 interactions.
STRING511145.b0038.

Proteomic databases

PRIDEP31572.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73149; AAC73149; b0038.
BAB96607; BAB96607; BAB96607.
GeneID12932590.
948997.
KEGGecj:Y75_p0038.
eco:b0038.
PATRIC32115171. VBIEscCol129921_0037.

Organism-specific databases

EchoBASEEB1520.
EcoGeneEG11559. caiB.

Phylogenomic databases

eggNOGCOG1804.
HOGENOMHOG000219745.
KOK08298.
OMAPLRMQNV.
OrthoDBEOG6Q2SGC.
PhylomeDBP31572.

Enzyme and pathway databases

BioCycEcoCyc:CARNDEHYDRA-MONOMER.
ECOL316407:JW0037-MONOMER.
MetaCyc:CARNDEHYDRA-MONOMER.
UniPathwayUPA00117.

Gene expression databases

GenevestigatorP31572.

Family and domain databases

Gene3D3.40.50.10540. 2 hits.
HAMAPMF_01050. CaiB.
InterProIPR003673. CoA-Trfase_fam_III.
IPR023452. CoA-Trfase_fam_III_CaiB.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]
PANTHERPTHR11837. PTHR11837. 1 hit.
PfamPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF89796. SSF89796. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP31572.
PROP31572.

Entry information

Entry nameCAIB_ECOLI
AccessionPrimary (citable) accession number: P31572
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene