Reviewed, UniProtKB/Swiss-Prot P60584 (CAIA_ECOLI)

Names and origin

Protein names

Recommended name:
    Crotonobetainyl-CoA dehydrogenase
    EC=1.3.99.-
Alternative name(s):
    Crotonobetainyl-CoA reductase

Gene names

Name:	caiA
Synonyms:	yaaO
Ordered Locus Names:	b0039, JW0038

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reduction of crotonobetainyl-CoA to gamma-butyrobetainyl-CoA. HAMAP MF_01052
Cofactor	Binds 1 FAD per subunit. Ref.5
Pathway	Amine and polyamine metabolism; carnitine metabolism. HAMAP MF_01052
Subunit structure	Homotetramer. Ref.5
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: HAMAP electron carrier activity 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 – 380	380	Crotonobetainyl-CoA dehydrogenase HAMAP MF_01052		PRO_0000201193

Sequences

	Sequence		Length	Mass (Da)
	P60584-1 [UniParc]. Last modified March 15, 2004. Version 1. Checksum: 7076984D735652C3	FASTA	380	42,558
	10 20 30 40 50 60 MDFNLNDEQE LFVAGIRELM ASENWEAYFA ECDRDSVYPE RFVKALADMG IDSLLIPEEH 70 80 90 100 110 120 GGLDAGFVTL AAVWMELGRL GAPTYVLYQL PGGFNTFLRE GTQEQIDKIM AFRGTGKQMW 130 140 150 160 170 180 NSAITEPGAG SDVGSLKTTY TRRNGKIYLN GSKCFITSSA YTPYIVVMAR DGASPDKPVY 190 200 210 220 230 240 TEWFVDMSKP GIKVTKLEKL GLRMDSCCEI TFDDVELDEK DMFGREGNGF NRVKEEFDHE 250 260 270 280 290 300 RFLVALTNYG TAMCAFEDAA RYANQRVQFG EAIGRFQLIQ EKFAHMAIKL NSMKNMLYEA 310 320 330 340 350 360 AWKADNGTIT SGDAAMCKYF CANAAFEVVD SAMQVLGGVG IAGNHRISRF WRDLRVDRVS 370 380 GGSDEMQILT LGRAVLKQYR

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]. 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 143 AND 182. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Crotonobetaine reductase from Escherichia coli consists of two proteins." Preusser A., Wagner U., Elssner T., Kleber H.-P. Biochim. Biophys. Acta 1431:166-178(1999) [PubMed: 10209289] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20, COFACTOR, SUBUNIT.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X73904 Genomic DNA. Translation: CAA52111.1. U00096 Genomic DNA. Translation: AAC73150.1. AP009048 Genomic DNA. Translation: BAB96608.2.
PIR	I41011. G64724.
RefSeq	AP_000703.1. NP_414581.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	949064.
GenomeReviews	Gene locus JW0038 in contig AP009048_GR. Gene locus b0039 in contig U00096_GR.
KEGG	ecj:JW0038. eco:b0039.
Organism-specific databases
EchoBASE	EB1521.
EcoGene	EG11560. caiA.
CMR	Search...
Phylogenomic databases
HOGENOM	P60584.
OMA	P60584. IFTEWFV.
Enzyme and pathway databases
BioCyc	EcoCyc:CROBETREDUCT-MON. MetaCyc:CROBETREDUCT-MON.
Family and domain databases
HAMAP	MF_01052. [Tree]
InterPro	IPR006089. Acyl-CoA_DH_CS. IPR006092. Acyl-CoA_DH_N. IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
PROSITE	PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAIA_ECOLI

Accession

Primary (citable) accession number: P60584
Secondary accession number(s): P31571

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	March 15, 2004
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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