P60584 (CAIA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reduction of crotonobetainyl-CoA to gamma-butyrobetainyl-CoA. HAMAP-Rule MF_01052
Cofactor	Binds 1 FAD per subunit. Ref.5
Pathway	Amine and polyamine metabolism; carnitine metabolism. HAMAP-Rule 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 Reference proteome
Gene Ontology (GO)
Biological_process	carnitine metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: HAMAP flavin adenine dinucleotide binding 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-Rule MF_01052		PRO_0000201193

Sequences

	Sequence		Length	Mass (Da)
	P60584 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20, COFACTOR, SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X73904 Genomic DNA. Translation: CAA52111.1. U00096 Genomic DNA. Translation: AAC73150.1. AP009048 Genomic DNA. Translation: BAB96608.2.
PIR	I41011. G64724.
RefSeq	NP_414581.1. NC_000913.2. YP_488345.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P60584.
SMR	P60584. Positions 5-377.
ModBase	Search...
Protein-protein interaction databases
IntAct	P60584. 5 interactions.
STRING	511145.b0039.
Proteomic databases
PRIDE	P60584.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73150; AAC73150; b0039. BAB96608; BAB96608; BAB96608.
GeneID	12934355. 949064.
KEGG	ecj:Y75_p0039. eco:b0039.
PATRIC	32115173. VBIEscCol129921_0038.
Organism-specific databases
EchoBASE	EB1521.
EcoGene	EG11560. caiA.
Phylogenomic databases
eggNOG	COG1960.
HOGENOM	HOG000131659.
KO	K08297.
OMA	YSAAIVW.
ProtClustDB	PRK03354.
Enzyme and pathway databases
BioCyc	EcoCyc:CROBETREDUCT-MONOMER. ECOL316407:JW0038-MONOMER. MetaCyc:CROBETREDUCT-MONOMER.
UniPathway	UPA00117.
Gene expression databases
Genevestigator	P60584.
Family and domain databases
Gene3D	1.10.540.10. 1 hit. 2.40.110.10. 1 hit.
HAMAP	MF_01052. CaiA.
InterPro	IPR006089. Acyl-CoA_DH_CS. IPR006092. Acyl-CoA_DH_N. IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_cen-dom. IPR009075. AcylCo_DH/oxidase_C. IPR013786. AcylCoA_DH/ox_N. IPR009100. AcylCoA_DH/oxidase. IPR023450. Crotonobetainyl-CoA_DHase_CaiA. [Graphical view]
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
SUPFAM	SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 1 hit.
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:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program