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Protein

L-carnitine CoA-transferase

Gene

caiB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA.
4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA.

Pathway: carnitine metabolism

This protein is involved in the pathway carnitine metabolism, which is part of Amine and polyamine metabolism.
View all proteins of this organism that are known to be involved in the pathway carnitine metabolism and in Amine and polyamine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971Coenzyme A1 Publication
Binding sitei104 – 1041Coenzyme A1 Publication
Active sitei169 – 1691Nucleophile

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciEcoCyc:CARNDEHYDRA-MONOMER.
ECOL316407:JW0037-MONOMER.
MetaCyc:CARNDEHYDRA-MONOMER.
BRENDAi2.8.3.21. 2026.
UniPathwayiUPA00117.

Names & Taxonomyi

Protein namesi
Recommended name:
L-carnitine CoA-transferase (EC:2.8.3.21)
Alternative name(s):
Crotonobetainyl-CoA:carnitine CoA-transferase
Gene namesi
Name:caiB
Synonyms:yaaN
Ordered Locus Names:b0038, JW0037
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11559. caiB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 405405L-carnitine CoA-transferasePRO_0000194708Add
BLAST

Proteomic databases

PRIDEiP31572.

Expressioni

Inductioni

By L-carnitine or crotonobetaine.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP31572. 12 interactions.
STRINGi511145.b0038.

Structurei

Secondary structure

1
405
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 144Combined sources
Beta strandi16 – 205Combined sources
Helixi25 – 3511Combined sources
Beta strandi39 – 446Combined sources
Beta strandi46 – 483Combined sources
Helixi51 – 544Combined sources
Beta strandi55 – 573Combined sources
Helixi58 – 625Combined sources
Turni63 – 653Combined sources
Beta strandi67 – 715Combined sources
Beta strandi73 – 753Combined sources
Helixi76 – 8611Combined sources
Beta strandi90 – 956Combined sources
Beta strandi97 – 993Combined sources
Helixi100 – 1034Combined sources
Helixi108 – 1147Combined sources
Beta strandi119 – 1268Combined sources
Beta strandi128 – 1303Combined sources
Turni132 – 1365Combined sources
Helixi141 – 1477Combined sources
Helixi151 – 1533Combined sources
Beta strandi154 – 1563Combined sources
Turni164 – 1663Combined sources
Helixi167 – 19024Combined sources
Beta strandi194 – 1996Combined sources
Helixi200 – 2078Combined sources
Helixi209 – 2168Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi244 – 2496Combined sources
Helixi253 – 26311Combined sources
Helixi266 – 2683Combined sources
Beta strandi271 – 2744Combined sources
Turni283 – 2853Combined sources
Helixi289 – 30113Combined sources
Helixi305 – 31410Combined sources
Beta strandi318 – 3214Combined sources
Helixi325 – 3273Combined sources
Helixi332 – 3376Combined sources
Beta strandi340 – 3445Combined sources
Beta strandi350 – 3545Combined sources
Beta strandi361 – 3633Combined sources
Turni374 – 3774Combined sources
Helixi378 – 3847Combined sources
Helixi389 – 3979Combined sources
Beta strandi400 – 4023Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP31572.
SMRiP31572. Positions 1-405.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31572.

Family & Domainsi

Sequence similaritiesi

Belongs to the CaiB/BaiF CoA-transferase family.Curated

Phylogenomic databases

eggNOGiCOG1804.
HOGENOMiHOG000219745.
InParanoidiP31572.
KOiK08298.
OMAiDMAIIEP.
OrthoDBiEOG6Q2SGC.
PhylomeDBiP31572.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
HAMAPiMF_01050. CaiB.
InterProiIPR023452. CoA-Trfase_CaiB.
IPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]
PANTHERiPTHR11837. PTHR11837. 1 hit.
PfamiPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.

Sequencei

Sequence statusi: Complete.

P31572-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD
60 70 80 90 100
TIRVQPNYPQ LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA
110 120 130 140 150
FARRGITDEV LWQHNPKLVI AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY
160 170 180 190 200
LIQNGDVDQP MPAFPYTADY FSGLTATTAA LAALHKVRET GKGESIDIAM
210 220 230 240 250
YEVMLRMGQY FMMDYFNGGE MCPRMSKGKD PYYAGCGLYK CADGYIVMEL
260 270 280 290 300
VGITQIEECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL
310 320 330 340 350
ATHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT
360 370 380 390 400
CKGPNIMPKF KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL

AKVED
Length:405
Mass (Da):45,127
Last modified:February 1, 1995 - v3
Checksum:i75583684B4B5A2DE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti187 – 1871V → A in strain: O44:K74.
Natural varianti302 – 3021T → A in strain: O44:K74.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67748 Genomic DNA. Translation: CAA47971.1.
X73904 Genomic DNA. Translation: CAA52112.1.
U00096 Genomic DNA. Translation: AAC73149.1.
AP009048 Genomic DNA. Translation: BAB96607.1.
PIRiS40559.
RefSeqiNP_414580.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC73149; AAC73149; b0038.
BAB96607; BAB96607; BAB96607.
GeneIDi948997.
KEGGiecj:Y75_p0038.
eco:b0038.
PATRICi32115171. VBIEscCol129921_0037.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67748 Genomic DNA. Translation: CAA47971.1.
X73904 Genomic DNA. Translation: CAA52112.1.
U00096 Genomic DNA. Translation: AAC73149.1.
AP009048 Genomic DNA. Translation: BAB96607.1.
PIRiS40559.
RefSeqiNP_414580.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP31572.
SMRiP31572. Positions 1-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP31572. 12 interactions.
STRINGi511145.b0038.

Proteomic databases

PRIDEiP31572.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73149; AAC73149; b0038.
BAB96607; BAB96607; BAB96607.
GeneIDi948997.
KEGGiecj:Y75_p0038.
eco:b0038.
PATRICi32115171. VBIEscCol129921_0037.

Organism-specific databases

EchoBASEiEB1520.
EcoGeneiEG11559. caiB.

Phylogenomic databases

eggNOGiCOG1804.
HOGENOMiHOG000219745.
InParanoidiP31572.
KOiK08298.
OMAiDMAIIEP.
OrthoDBiEOG6Q2SGC.
PhylomeDBiP31572.

Enzyme and pathway databases

UniPathwayiUPA00117.
BioCyciEcoCyc:CARNDEHYDRA-MONOMER.
ECOL316407:JW0037-MONOMER.
MetaCyc:CARNDEHYDRA-MONOMER.
BRENDAi2.8.3.21. 2026.

Miscellaneous databases

EvolutionaryTraceiP31572.
PROiP31572.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
HAMAPiMF_01050. CaiB.
InterProiIPR023452. CoA-Trfase_CaiB.
IPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]
PANTHERiPTHR11837. PTHR11837. 1 hit.
PfamiPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCAIB_ECOLI
AccessioniPrimary (citable) accession number: P31572
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1995
Last modified: June 24, 2015
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Caution

Was originally thought to be an L-carnitine dehydratase.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.