Identification
Name:3-phenylpropionate/cinnamic acid dioxygenase subunit alpha
Synonyms:
  • Digoxigenin subunit alpha
Gene Name:hcaE
Enzyme Class:
Biological Properties
General Function:Involved in iron ion binding
Specific Function:Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Microbial metabolism in diverse environments ec01120
  • Phenylalanine metabolism ec00360
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.03-phenylpropanoate1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.03-phenylpropanoate1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB21422Cinnamic acidMetaboCard
ECMDB20129cis-3-(3-Carboxyethenyl)-3,5-cyclohexadiene-1,2-diolMetaboCard
ECMDB21320Cis-3-(3-carboxyethyl)-3,5-cyclohexadiene-1,2-diolMetaboCard
ECMDB20130cis-3-(Carboxy-ethyl)-3,5-cyclo-hexadiene-1,2-diolMetaboCard
ECMDB00764Hydrocinnamic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB20197Trans-2,3-DihydroxycinnamateMetaboCard
ECMDB00930trans-Cinnamic acidMetaboCard
GO Classification:
Function
2 iron, 2 sulfur cluster binding
3-phenylpropionate dioxygenase activity
binding
catalytic activity
cation binding
ion binding
iron ion binding
iron-sulfur cluster binding
metal cluster binding
metal ion binding
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor
transition metal ion binding
Process
aromatic compound catabolic process
cellular aromatic compound metabolic process
cellular metabolic process
metabolic process
oxidation reduction
Gene Properties
Blattner:b2538
Gene OrientationClockwise
Centisome Percentage:57.48
Left Sequence End2667054
Right Sequence End2668415
Gene Sequence:
>1362 bp
ATGTCTTTTGATTTAATCATTAAAAACGGCACCGTTATTTTAGAAAACGAAGCTCGCGTT
GTAGATATCGCCGTTAAAGGCGGAAAAATTGCTGCTATCGGTCAGGATCTGGGCGATGCA
AAAGAAGTTATGGATGCGTCTGGTCTGGTGGTTTCGCCGGGCATGGTTGATGCGCACACC
CATATTTCTGAACCGGGTCGTAGCCACTGGGAAGGTTATGAAACCGGTACTCGCGCAGCG
GCAAAAGGTGGTATCACCACCATGATCGAAATGCCGCTCAACCAGCTGCCTGCAACGGTT
GACCGCGCTTCAATTGAACTGAAGTTCGATGCCGCTAAAGGCAAGCTGACTATTGATGCG
GCACAACTCGGTGGCCTGGTGTCTTACAACATCGACCGTCTGCATGAGCTGGATGAAGTG
GGCGTTGTCGGCTTCAAATGCTTCGTTGCGACCTGTGGCGATCGCGGTATCGACAACGAC
TTCCGTGATGTAAACGACTGGCAGTTCTTCAAAGGTGCGCAGAAGCTGGGCGAACTGGGT
CAGCCGGTGCTGGTGCACTGCGAAAACGCGCTGATTTGTGACGAACTGGGCGAAGAAGCG
AAGCGTGAAGGTCGCGTAACCGCTCATGACTATGTGGCTTCGCGTCCGGTATTTACCGAA
GTGGAAGCAATTCGCCGCGTACTGTATCTGGCGAAAGTTGCTGGTTGCCGTCTGCACGTT
TGCCACGTCAGCAGCCCGGAAGGTGTTGAGGAAGTGACTCGTGCACGTCAGGAAGGTCAG
GACGTTACTTGTGAATCCTGCCCGCATTACTTTGTACTGGATACCGATCAGTTCGAAGAA
ATCGGTACTCTGGCGAAGTGTTCACCGCCGATCCGCGATCTGGAAAACCAGAAAGGCATG
TGGGAAAAACTGTTTAACGGTGAAATCGACTGCCTGGTTTCCGACCACTCTCCATGCCCG
CCGGAAATGAAAGCCGGTAACATCATGAAAGCATGGGGCGGTATCGCCGGTCTGCAAAGC
TGCATGGACGTGATGTTCGATGAAGCGGTACAGAAACGCGGTATGTCTCTGCCAATGTTC
GGCAAATTAATGGCGACTAACGCAGCAGATATTTTCGGTCTGCAGCAAAAAGGCCGTATC
GCCCCAGGAAAAGATGCCGACTTCGTCTTCATTCAGCCGAATAGCAGCTATGTTCTTACC
AATGACGATCTGGAATATCGCCACAAAGTCAGCCCGTATGTTGGCCGTACCATTGGCGCG
CGTATCACGAAAACCATCTTACGTGGTGATGTGATTTACGACATTGAACAGGGCTTCCCT
GTTGCGCCGAAAGGTCAATTTATCCTTAAACATCAGCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:453
Protein Molecular Weight:51109
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3-phenylpropionate/cinnamic acid dioxygenase subunit alpha
MTTPSDLNIYQLIDTQNGRVTPRIYTDPDIYQLELERIFGRCWLFLAHESQIPKPGDFFN
TYMGEDAVVVVRQKDGSIKAFLNQCRHRAMRVSYADCGNTRAFTCPYHGWSYGINGELID
VPLEPRAYPQGLCKSHWGLNEVPCVESYKGLIFGNWDTSAPGLRDYLGDIAWYLDGMLDR
REGGTEIVGGVQKWVINCNWKFPAEQFASDQYHALFSHASAVQVLGAKDDGSDKRLGDGQ
TARPVWETAKDALQFGQDGHGSGFFFTEKPDANVWVDGAVSSYYRETYAEAEQRLGEVRA
LRLAGHNNIFPTLSWLNGTATLRVWHPRGPDQVEVWAFCITDKAASDEVKAAFENSATRA
FGPAGFLEQDDSENWCEIQKLLKGHRARNSKLCLEMGLGQEKRRDDGIPGITNYIFSETA
ARGMYQRWADLLSSESWQEVLDKTAAYQQEVMK
References
External Links:
ResourceLink
Uniprot ID:P0ABR5
Uniprot Name:HCAE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674650
Ecogene ID:EG13456
Ecocyc:EG13456
ColiBase:b2538
Kegg Gene:b2538
EchoBASE ID:EB3229
CCDB:HCAE_ECOLI
BacMap:16130463
General Reference:
  • 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
  • Diaz, E., Ferrandez, A., Garcia, J. L. (1998). "Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12." J Bacteriol 180:2915-2923. Pubmed: 9603882
  • 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
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837