Reviewed, UniProtKB/Swiss-Prot Q83K39 (HCAE_SHIFL)

Names and origin

Protein names

Recommended name:
    3-phenylpropionate/cinnamic acid dioxygenase subunit alpha
    EC=1.14.12.19
Alternative name(s):
    Digoxigenin subunit alpha

Gene names

Name:	hcaE
Ordered Locus Names:	SF2585, S2757

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

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 By similarity. HAMAP MF_01648
Catalytic activity	3-phenylpropanoic acid + NADH + O2 = cis-3-(2-carboxyethyl)-3,5-cyclohexadiene-1,2-diol + NAD+. HAMAP MF_01648 Cinnamic acid + H+ + NADH + O2 = cis-3-(2-carboxyethenyl)-3,5-cyclohexadiene-1,2-diol + NAD+. HAMAP MF_01648
Cofactor	Binds 1 iron ion By similarity. HAMAP MF_01648 Binds 1 2Fe-2S cluster per subunit By similarity. HAMAP MF_01648
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01648
Subunit structure	This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (hcaE and hcaF), a ferredoxin (hcaC) and a ferredoxin reductase (hcaD) By similarity. HAMAP MF_01648
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. Contains 1 Rieske domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding NAD
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3-phenylpropionate dioxygenase activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 453	453	3-phenylpropionate/cinnamic acid dioxygenase subunit alpha HAMAP MF_01648		PRO_0000333707
Regions
	Domain	44 – 142	99	Rieske
Sites
	Metal binding	85	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	87	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	105	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	108	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	213	1	Iron By similarity
	Metal binding	218	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q83K39-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: C1EB5F940708316C	FASTA	453	51,076
	10 20 30 40 50 60 MTTPSDLNIY QLIDTQNGRV TPRIYTDPDI YQLELERIFG RCWLFLAHES QIPKPGDFFN 70 80 90 100 110 120 TYMGEDAVVV VRQKDGSIKA FLNQCRHRAM RVSYADCGNS RAFTCPYHGW SYGINGELID 130 140 150 160 170 180 VPLEPRAYPQ GLCKSHWGLN EVPCVESYKG LIFGNWDTSA PGLHDYLGDI 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

References

[1]

"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.

[2]

"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005674 Genomic DNA. Translation: AAN44084.1. AE014073 Genomic DNA. Translation: AAP17909.1.
RefSeq	NP_708377.1. NP_838099.1.
3D structure databases
HSSP	HSSP built from PDB template 2B1X based on UniProtKB Q9X3R9.
SMR	Q83K39. Positions 6-440.
ModBase	Search...
Genome annotation databases
GeneID	1026946. 1078029.
GenomeReviews	Gene locus SF2585 in contig AE005674_GR. Gene locus S2757 in contig AE014073_GR.
KEGG	sfl:SF2585. sfx:S2757.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG705920.
OMA	GESTEAR.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN44084.1-MONOMER.
Family and domain databases
HAMAP	MF_01648. HcaE. [Tree]
InterPro	IPR020875. Digoxigenin_alpha-su. IPR017941. Rieske_2Fe-2S. IPR015881. Ring-hydroxy_dOase_2Fe2S_BS. IPR015879. Ring_hydroxy_dOase_asu_C. IPR001663. Rng_hydr_dOase-A. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
PANTHER	PTHR21266:SF2. Rng_hydr_dOase-A. 1 hit.
Pfam	PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view]
PRINTS	PR00090. RNGDIOXGNASE.
PROSITE	PS51296. RIESKE. 1 hit. PS00570. RING_HYDROXYL_ALPHA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HCAE_SHIFL

Accession

Primary (citable) accession number: Q83K39
Secondary accession number(s): Q7C0G4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	June 1, 2003
Last modified:	January 19, 2010
This is version 54 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)