Crotonobetainyl-CoA:carnitine CoA-transferase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P31572 (CAIB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Crotonobetainyl-CoA:carnitine CoA-transferase
EC=2.8.3.-

Gene names

Name:	caiB
Synonyms:	yaaN
Ordered Locus Names:	b0038, JW0037

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	405 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP MF_01050
Pathway	Amine and polyamine metabolism; carnitine metabolism. HAMAP MF_01050
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP MF_01050.
Induction	By L-carnitine or crotonobetaine. HAMAP MF_01050
Miscellaneous	Some strains of E.coli, such as ATCC 25922, can metabolize carnitine under aerobiosis. HAMAP MF_01050
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 component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	carnitine catabolic process Inferred from experiment Ref.1. Source: EcoliWiki
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carnitine dehydratase activity Inferred from experiment Ref.2 Ref.1. Source: EcoliWiki transferase activity, transferring sulfur-containing groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 405

405

Crotonobetainyl-CoA:carnitine CoA-transferase HAMAP MF_01050

PRO_0000194708

Sites

Active site

169

Nucleophile

Binding site

Coenzyme A

Binding site

104

Coenzyme A

Natural variations

Natural variant

187

V → A in strain: O44:K74.

Natural variant

302

T → A in strain: O44:K74.

Secondary structure

405

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P31572 [UniParc].

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

FASTA

405

45,127

        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' referencesShow '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: 8188598] [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: 7815937] [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: 1630901] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 11551212] [Abstract] Cited for: CHARACTERIZATION. 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: 10339822] [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: 15518548] [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.

PIR

S40559.

RefSeq

NP_414580.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XA3	X-ray	1.85	A/B	2-405	[»]
1XA4	X-ray	1.90	A/B	2-405	[»]
1XK6	X-ray	1.85	A/B/C/D	1-405	[»]
1XK7	X-ray	1.60	A/B/C	1-405	[»]
1XVT	X-ray	2.30	A	1-405	[»]
1XVU	X-ray	2.40	A	1-405	[»]
1XVV	X-ray	2.40	A	1-405	[»]

ProteinModelPortal

P31572.

SMR

P31572. Positions 1-405.

ModBase

Search...

Protein-protein interaction databases

IntAct

P31572. 11 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003222; EBESCP00000003222; EBESCG00000002647.
EBESCT00000018210; EBESCP00000017501; EBESCG00000017265.

GeneID

948997.

GenomeReviews

Gene locus JW0037 in contig AP009048_GR.
Gene locus b0038 in contig U00096_GR.

KEGG

ecj:JW0037.
eco:b0038.

PATRIC

32115171. VBIEscCol129921_0037.

Organism-specific databases

EchoBASE

EB1520.

EcoGene

EG11559. caiB.

Phylogenomic databases

eggNOG

COG1804.

GeneTree

EBGT00050000009654.

HOGENOM

HBG659028.

OMA

IDVAMYE.

PhylomeDB

P31572.

ProtClustDB

PRK03525.

Enzyme and pathway databases

BioCyc

EcoCyc:CARNDEHYDRA-MONOMER.
MetaCyc:CARNDEHYDRA-MONOMER.

Gene expression databases

Genevestigator

P31572.

Family and domain databases

HAMAP

MF_01050. CaiB.
[Tree]

InterPro

IPR003673. CoA-Trfase_fam_III.
IPR023452. CoA-Trfase_fam_III_CaiB.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.10540. CoA-Trfase_fam_III. 1 hit.

K08298.

PANTHER

PTHR11837. CAIB_BAIF. 1 hit.

Pfam

PF02515. CoA_transf_3. 1 hit.
[Graphical view]

SUPFAM

SSF89796. CoA-Trfase_fam_III. 1 hit.

ProtoNet

Search...

Entry information

Entry name

CAIB_ECOLI

Accession

Primary (citable) accession number: P31572

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents