Reviewed, UniProtKB/Swiss-Prot Q0T1Y1 (HCAE_SHIF8)

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:	SFV_2586

Organism

Shigella flexneri serotype 5b (strain 8401) [Complete proteome] [HAMAP]

Taxonomic identifier

373384 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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. Binds 1 2Fe-2S cluster per subunit By similarity.
Pathway	Aromatic compound metabolism; 3-phenylpropionic acid 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.
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 electron carrier activity Inferred from electronic annotation. Source: InterPro 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_0000333708
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)
	Q0T1Y1-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 2C36276567B57045	FASTA	453	51,120
	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 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 DQVEVWTFCI TDKAASDEVK AAFENSATRA 370 380 390 400 410 420 FGPAGFLEQD DSENWCEIQK LLKGHRARNS KLCLEMGLGQ EKRRDDGIPG ITNYIFSETA 430 440 450 ARGMYQRWAD LLSSESWQEV LDKTAAYQQE VMK

References

[1]

"Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a." Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q. BMC Genomics 7:173-173(2006) [PubMed: 16822325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000266 Genomic DNA. Translation: ABF04684.1.
RefSeq	YP_689989.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4207321.
GenomeReviews	Gene locus SFV_2586 in contig CP000266_GR.
KEGG	sfv:SFV_2586.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0T1Y1.
OMA	Q0T1Y1. LEMEFIF.
Enzyme and pathway databases
BioCyc	SFLE373384:SFV_2586-MON.
Family and domain databases
HAMAP	MF_01648. [Tree]
InterPro	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_SHIF8

Accession

Primary (citable) accession number: Q0T1Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 27 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)