Q31XV2 (HCAE_SHIBS) Reviewed, UniProtKB/Swiss-Prot

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:	SBO_2562

Organism

Shigella boydii serotype 4 (strain Sb227) [Complete proteome] [HAMAP]

Taxonomic identifier

300268 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella › Shigella boydii

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-Rule MF_01648
Catalytic activity	3-phenylpropanoate + NADH + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+. HAMAP-Rule MF_01648 (2E)-3-phenylprop-2-enoate + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD+. HAMAP-Rule MF_01648
Cofactor	Binds 1 iron ion By similarity. Binds 1 2Fe-2S cluster per subunit By similarity.
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule 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	3-phenylpropionate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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-Rule MF_01648		PRO_0000333706
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)
	Q31XV2 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 43535BF0F57643F4	FASTA	453	51,049
	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 KSPAEQFASD 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 dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery." Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q. Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sb227.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000036 Genomic DNA. Translation: ABB67106.1.
RefSeq	YP_408934.1. NC_007613.1.
3D structure databases
ProteinModelPortal	Q31XV2.
ModBase	Search...
Protein-protein interaction databases
STRING	300268.SBO_2562.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABB67106; ABB67106; SBO_2562.
GeneID	3781545.
KEGG	sbo:SBO_2562.
PATRIC	18684554. VBIShiBoy33460_3184.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4638.
HOGENOM	HOG000105925.
KO	K05708.
OMA	FRIARNM.
ProtClustDB	CLSK880425.
Enzyme and pathway databases
BioCyc	SBOY300268:GJFL-2559-MONOMER.
UniPathway	UPA00714.
Family and domain databases
Gene3D	2.102.10.10. 1 hit.
HAMAP	MF_01648. HcaE.
InterPro	IPR020875. HcaE. IPR017941. Rieske_2Fe-2S. IPR015881. Ring-hydroxy_dOase_2Fe2S_BS. IPR015879. Ring_hydroxy_dOase_asu_C_dom. IPR001663. Rng_hydr_dOase-A. [Graphical view]
Pfam	PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view]
PRINTS	PR00090. RNGDIOXGNASE.
SUPFAM	SSF50022. Rieske_dom. 1 hit.
PROSITE	PS51296. RIESKE. 1 hit. PS00570. RING_HYDROXYL_ALPHA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HCAE_SHIBS

Accession

Primary (citable) accession number: Q31XV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program