P31551 (CAID_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carnitinyl-CoA dehydratase
EC=4.2.1.-

Alternative name(s):
Crotonobetainyl-CoA hydratase

Gene names

Name:	caiD
Synonyms:	yaaL
Ordered Locus Names:	b0036, JW0035

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. HAMAP MF_01051
Catalytic activity	L-carnitinyl-CoA = H2O + crotonobetainyl-CoA. HAMAP MF_01051
Pathway	Amine and polyamine metabolism; carnitine metabolism. HAMAP MF_01051
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.
Sequence caution	The sequence BAB96605.2 differs from that shown. Reason: Erroneous initiation. The sequence CAA52114.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carnitine catabolic process Ref.1 Inferred from Experiment. Source: EcoliWiki
Molecular function	carnitine racemase activity Ref.1 Inferred from Experiment. Source: EcoliWiki lyase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 261	260	Carnitinyl-CoA dehydratase HAMAP MF_01051		PRO_0000109348
Sites
	Site	111	1	Important for catalytic activity By similarity
	Site	131	1	Important for catalytic activity By similarity
Natural variations
	Natural variant	247	1	P → L in strain: O44:K74.

Sequences

	Sequence		Length	Mass (Da)
	P31551-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 2C4DD6C3D16995CC	FASTA	261	28,190
	10 20 30 40 50 60 MSESLHLTRN GSILEITLDR PKANAIDAKT SFEMGEVFLN FRDDPQLRVA IITGAGEKFF 70 80 90 100 110 120 SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FNLDKPVIAA VNGYAFGGGF ELALAADFIV 130 140 150 160 170 180 CADNASFALP EAKLGIVPDS GGVLRLPKIL PPAIVNEMVM TGRRMGAEEA LRWGIVNRVV 190 200 210 220 230 240 SQAELMDNAR ELAQQLVNSA PLAIAALKEI YRTTSEMPVE EAYRYIRSGV LKHYPSVLHS 250 260 EDAIEGPLAF AEKRDPVWKG R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], CHARACTERIZATION. Strain: O44:K74.
[2]	"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.
[3]	"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.
[4]	"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], SEQUENCE REVISION TO 108. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"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: PROTEIN SEQUENCE OF 2-11, CHARACTERIZATION. Strain: O44:K74.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X73904 Genomic DNA. Translation: CAA52114.1. Different initiation. U00096 Genomic DNA. Translation: AAC73147.2. AP009048 Genomic DNA. Translation: BAB96605.2. Different initiation.
PIR	D64724.
RefSeq	AP_000700.1. NP_414578.2.
3D structure databases
ProteinModelPortal	P31551.
SMR	P31551. Positions 3-261.
ModBase	Search...
Protein-protein interaction databases
STRING	P31551.
Genome annotation databases
EnsemblBacteria	EBESCT00000002919; EBESCP00000002919; EBESCG00000002385. EBESCT00000014749; EBESCP00000014040; EBESCG00000013809.
GeneID	948995.
GenomeReviews	Gene locus JW0035 in contig AP009048_GR. Gene locus b0036 in contig U00096_GR.
KEGG	ecj:JW0035. eco:b0036.
Organism-specific databases
EchoBASE	EB1518.
EcoGene	EG11557. caiD.
CMR	Search...
Phylogenomic databases
eggNOG	COG1024.
HOGENOM	HBG748731.
OMA	PDSGGML.
ProtClustDB	PRK03580.
Enzyme and pathway databases
BioCyc	EcoCyc:CARNRACE-MONOMER. MetaCyc:CARNRACE-MONOMER.
Gene expression databases
Genevestigator	P31551.
Family and domain databases
HAMAP	MF_01051. CaiD. [Tree]
InterPro	IPR001753. Crotonase_core. IPR018376. Enoyl-CoA_hyd/isom_CS. [Graphical view]
Pfam	PF00378. ECH. 1 hit. [Graphical view]
PROSITE	PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAID_ECOLI

Accession

Primary (citable) accession number: P31551
Secondary accession number(s): P75623

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	August 10, 2010
This is version 94 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)