ECMDB: Beta-ketoadipyl-CoA thiolase (P0C7L2)

Identification

Name:

Beta-ketoadipyl-CoA thiolase

Synonyms:

3-oxoadipyl-CoA thiolase

Gene Name:

paaJ

Enzyme Class:

Biological Properties

General Function:

Involved in transferase activity, transferring acyl groups other than amino-acyl groups

Specific Function:

Catalyzes thiolytic cleavage of beta-ketoadipyl-CoA to succinyl-CoA and acetyl-CoA

Cellular Location:

Not Available

SMPDB Pathways:

Phenylalanine metabolism PW000921
Phenylethylamine metabolism PW002027

KEGG Pathways:

Benzoate degradation via hydroxylation ec00362
Microbial metabolism in diverse environments ec01120
Phenylalanine metabolism ec00360

KEGG Reactions:

1.0

↔

1.0

1.03-Oxo-5,6-dehydrosuberyl-CoA + 1.0Coenzyme A ↔ 1.05-Carboxy-2-pentenoyl-CoA + 1.0Acetyl-CoA
ReactionCard

1.0

↔

1.0

1.0Coenzyme A + 1.03-Oxoadipyl-CoA ↔ 1.0Acetyl-CoA + 1.0Succinyl-CoA
ReactionCard

1.0

↔

1.0

1.0Succinyl-CoA + 1.0Acetyl-CoA ↔ 1.0Coenzyme A + 1.03-Oxoadipyl-CoA
ReactionCard

SMPDB Reactions:

1.0

→

1.0

1.02,3-didehydroadipyl-CoA

1.03-Oxo-5,6-dehydrosuberyl-CoA + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.02,3-didehydroadipyl-CoA
ReactionCard

1.03-Oxoadipyl-CoA

1.0

→

1.0

1.03-Oxoadipyl-CoA + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.0Succinyl-CoA
ReactionCard

EcoCyc Reactions:

1.0

↔

1.0

1.0Coenzyme A + 1.03-Oxoadipyl-CoA ↔ 1.0Acetyl-CoA + 1.0Succinyl-CoA
ReactionCard

1.0

←

1.0

1.0Succinyl-CoA + 1.0Acetyl-CoA ← 1.03-Oxoadipyl-CoA + 1.0Coenzyme A
ReactionCard

1.0

→

1.02,3-dehydroadipyl-CoA

1.0

1.03-Oxo-5,6-dehydrosuberyl-CoA + 1.0Coenzyme A → 1.02,3-dehydroadipyl-CoA + 1.0Acetyl-CoA
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB23163	2,3-dehydroadipyl-CoA	MetaboCard
ECMDB21172	3-Oxo-5,6-dehydrosuberyl-CoA	MetaboCard
ECMDB20077	3-Oxoadipyl-CoA	MetaboCard
ECMDB20101	5-Carboxy-2-pentenoyl-CoA	MetaboCard
ECMDB01206	Acetyl-CoA	MetaboCard
ECMDB01423	Coenzyme A	MetaboCard
ECMDB01022	Succinyl-CoA	MetaboCard

GO Classification:

Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
Process
catechol catabolic process
catechol metabolic process
cellular aromatic compound metabolic process
cellular metabolic process
metabolic process
phenol metabolic process
protocatechuate catabolic process

Gene Properties

Blattner:

b1397

Gene Orientation

Not Available

Centisome Percentage:

Not Available

Left Sequence End

Not Available

Right Sequence End

Not Available

Gene Sequence:

>1206 bp
ATGCGTGAAGCCTTTATTTGTGACGGAATTCGTACGCCAATTGGTCGCTACGGCGGGGCA
TTATCAAGTGTTCGGGCTGATGATCTGGCTGCTATCCCTTTGCGGGAACTGCTGGTGCGA
AACCCGCGTCTCGATGCGGAGTGTATCGATGATGTGATCCTCGGCTGTGCTAATCAGGCG
GGAGAAGATAACCGTAACGTAGCCCGGATGGCGACTTTACTGGCGGGGCTGCCGCAGAGT
GTTTCCGGCACAACCATTAACCGCTTGTGTGGTTCCGGGCTGGACGCACTGGGGTTTGCC
GCACGGGCGATTAAAGCGGGCGATGGCGATTTGCTGATCGCCGGTGGCGTGGAGTCAATG
TCACGGGCACCGTTTGTTATGGGCAAGGCAGCCAGTGCATTTTCTCGTCAGGCTGAGATG
TTCGATACCACTATTGGCTGGCGATTTGTGAACCCGCTCATGGCTCAGCAATTTGGAACT
GACAGCATGCCGGAAACGGCAGAGAATGTAGCTGAACTGTTAAAAATCTCACGAGAAGAT
CAAGATAGTTTTGCGCTACGCAGTCAGCAACGTACGGCAAAAGCGCAATCCTCAGGCATT
CTGGCTGAGGAGATTGTTCCGGTTGTGTTGAAAAACAAGAAAGGTGTTGTAACAGAAATA
CAACATGATGAGCATCTGCGCCCGGAAACGACGCTGGAACAGTTACGTGGGTTAAAAGCA
CCATTTCGTGCCAATGGGGTGATTACCGCAGGCAATGCTTCCGGGGTGAATGACGGAGCC
GCTGCGTTGATTATTGCCAGTGAACAGATGGCAGCAGCGCAAGGACTGACACCGCGGGCG
CGTATCGTAGCCATGGCAACCGCCGGGGTGGAACCGCGCCTGATGGGGCTTGGTCCGGTG
CCTGCAACTCGCCGGGTGCTGGAACGCGCAGGGCTGAGTATTCACGATATGGACGTGATT
GAACTGAACGAAGCGTTCGCGGCCCAGGCGTTGGGTGTACTACGCGAATTGGGGCTGCCT
GATGATGCCCCACATGTTAACCCCAACGGAGGCGCTATCGCCTTAGGCCATCCGTTGGGA
ATGAGTGGTGCCCGCCTGGCACTGGCTGCCAGCCATGAGCTGCATCGGCGTAACGGTCGT
TACGCATTGTGCACCATGTGCATCGGTGTCGGTCAGGGCATCGCCATGATTCTGGAGCGT
GTTTGA

Protein Properties

Pfam Domain Function:

Thiolase_C (PF02803 )
Thiolase_N (PF00108 )

Protein Residues:

401

Protein Molecular Weight:

42276

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Beta-ketoadipyl-CoA thiolase
MREAFICDGIRTPIGRYGGALSSVRADDLAAIPLRELLVRNPRLDAECIDDVILGCANQA
GEDNRNVARMATLLAGLPQSVSGTTINRLCGSGLDALGFAARAIKAGDGDLLIAGGVESM
SRAPFVMGKAASAFSRQAEMFDTTIGWRFVNPLMAQQFGTDSMPETAENVAELLKISRED
QDSFALRSQQRTAKAQSSGILAEEIVPVVLKNKKGVVTEIQHDEHLRPETTLEQLRGLKA
PFRANGVITAGNASGVNDGAAALIIASEQMAAAQGLTPRARIVAMATAGVEPRLMGLGPV
PATRRVLERAGLSIHDMDVIELNEAFAAQALGVLRELGLPDDAPHVNPNGGAIALGHPLG
MSGARLALAASHELHRRNGRYALCTMCIGVGQGIAMILERV

References

External Links:

Resource	Link
Uniprot ID:	P0C7L2
Uniprot Name:	PAAJ_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	1742272
ColiBase:	b1397
Kegg Gene:	b1397
EchoBASE ID:	EB3507
CCDB:	PAAJ_ECOLI
BacMap:	16129358

General Reference:

Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Ferrandez, A., Garcia, J. L., Diaz, E. (2000). "Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli." J Biol Chem 275:12214-12222. Pubmed: 10766858
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Nogales, J., Macchi, R., Franchi, F., Barzaghi, D., Fernandez, C., Garcia, J. L., Bertoni, G., Diaz, E. (2007). "Characterization of the last step of the aerobic phenylacetic acid degradation pathway." Microbiology 153:357-365. Pubmed: 17259607