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UniProtKB/Swiss-Prot entry P0ABR6

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HCAE_ECO57
Primary accession number P0ABR6
Secondary accession numbers P77590 P78203 Q47139
Integrated into Swiss-Prot on November 8, 2005
Sequence was last modified on November 8, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 27)
Name and origin of the protein
Protein name 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha
Synonyms EC 1.14.12.19
Digoxigenin subunit alpha
Gene name
Name: hcaE
OrderedLocusNames: Z3809, ECs3404
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE005174; AAG57651.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB36827.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D91054; D91054.
G85898; G85898.
RefSeq NP_289094.1; -.
NP_311431.1; -.
3D structure databases
HSSP P23094; 1O7N. [HSSP ENTRY / PDB]
ModBase P0ABR6.
Enzyme and pathway databases
BioCyc ECOL83334:ECS3404-MON; -.
Ontologies
GO
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0008695; Molecular function: 3-phenylpropionate dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0016702; Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0019439; Biological process: aromatic compound catabolic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_01648; -; 1.
PBIL [Tree]
InterPro IPR005806; Rieske_reg.
IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879; Ring_hydroxy_dOase_asu_C.
IPR001663; Rng_hydr_dOase-A.
Graphical view of domain structure.
Gene3D G3DSA:2.102.10.10; Rieske_reg; 1.
PANTHER PTHR21266:SF2; Rng_hydr_dOase-A; 1.
Pfam PF00355; Rieske; 1.
PF00848; Ring_hydroxyl_A; 1.
Pfam graphical view of domain structure.
PRINTS PR00090; RNGDIOXGNASE.
PROSITE PS51296; RIESKE; 1.
PS00570; RING_HYDROXYL_ALPHA; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 913881; -.
957853; -.
GenomeReviews AE005174_GR; Z3809.
BA000007_GR; ECs3404.
KEGG ece:Z3809; -.
ecs:ECs3404; -.
Phylogenomic databases
HOGENOM P0ABR6; -.
Genome annotation databases
CMR P0ABR6; Z3809.
Other
ProtoNet P0ABR6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   453  453     3-phenylpropionate/cinnamic acid dioxygenase subunit alpha. PRO_0000085062
DOMAIN   44   142  99     Rieske. 
METAL   85    85        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   87    87        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   105   105        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   108   108        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   213   213        Iron (By similarity). 
METAL   218   218        Iron (By similarity). 
Sequence information
Length: 453 AA [This is the length of the unprocessed precursor] Molecular weight: 51109 Da [This is the MW of the unprocessed precursor] CRC64: 02535BF5F47643FD [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTTPSDLNIY QLIDTQNGRV TPRIYTDPDI YQLELERIFG RCWLFLAHES QIPKPGDFFN 

        70         80         90        100        110        120 
TYMGEDAVVV VRQKDGSIKA FLNQCRHRAM RVSYADCGNT RAFTCPYHGW SYGINGELID 

       130        140        150        160        170        180 
VPLEPRAYPQ GLCKSHWGLN EVPCVESYKG LIFGNWDTSA PGLRDYLGDI AWYLDGMLDR 

       190        200        210        220        230        240 
REGGTEIVGG VQKWVINCNW KFPAEQFASD QYHALFSHAS AVQVLGAKDD GSDKRLGDGQ 

       250        260        270        280        290        300 
TARPVWETAK DALQFGQDGH GSGFFFTEKP DANVWVDGAV SSYYRETYAE AEQRLGEVRA 

       310        320        330        340        350        360 
LRLAGHNNIF PTLSWLNGTA TLRVWHPRGP DQVEVWAFCI TDKAASDEVK AAFENSATRA 

       370        380        390        400        410        420 
FGPAGFLEQD DSENWCEIQK LLKGHRARNS KLCLEMGLGQ EKRRDDGIPG ITNYIFSETA 

       430        440        450 
ARGMYQRWAD LLSSESWQEV LDKTAAYQQE VMK
P0ABR6 in FASTA format

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