Q83K38 (HCAF_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-phenylpropionate/cinnamic acid dioxygenase subunit beta
EC=1.14.12.19

Alternative name(s):
Digoxigenin subunit beta

Gene names

Name:	hcaF
Ordered Locus Names:	SF2586, S2758

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	172 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_01649
Catalytic activity	3-phenylpropanoate + NADH + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+. (2E)-3-phenylprop-2-enoate + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD+.
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01649
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 beta subunit family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	NAD
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-phenylpropionate dioxygenase activity Inferred from electronic annotation. Source: EC 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 – 172	172	3-phenylpropionate/cinnamic acid dioxygenase subunit beta HAMAP MF_01649		PRO_0000333715

Sequences

	Sequence		Length	Mass (Da)
	Q83K38 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 58203B22B5D97554	FASTA	172	20,565
	10 20 30 40 50 60 MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLAQLDEEI RYTMRTTVNA QTRDRRKGVQ 70 80 90 100 110 120 PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS NCQVSETDIP NVFAVRVNYL 130 140 150 160 170 LYRAQKERDE TFYVGTRFDK VRRLEDDNWR LLERDIVLDQ AVITSHNLSV LF

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: AAN44085.1. AE014073 Genomic DNA. Translation: AAP17910.1.
RefSeq	NP_708378.1. NC_004337.2. NP_838100.1. NC_004741.1.
3D structure databases
HSSP	HSSP built from PDB template 2B1X based on UniProtKB Q9WVZ0.
ProteinModelPortal	Q83K38.
SMR	Q83K38. Positions 2-172.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000086509; EBESCP00000083331; EBESCG00000085554. EBESCT00000090956; EBESCP00000087592; EBESCG00000090000.
GeneID	1025645. 1079025.
GenomeReviews	Gene locus SF2586 in contig AE005674_GR. Gene locus S2758 in contig AE014073_GR.
KEGG	sfl:SF2586. sfx:S2758.
PATRIC	18707148. VBIShiFle31049_3042.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000011518.
HOGENOM	HBG582498.
OMA	ARRTICV.
ProtClustDB	PRK10069.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN44085.1-MONOMER.
Family and domain databases
HAMAP	MF_01649. HcaF. [Tree]
InterPro	IPR023712. HcaF. IPR000391. Rng_hydr_dOase-bsu. [Graphical view]
KO	K05709.
Pfam	PF00866. Ring_hydroxyl_B. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HCAF_SHIFL

Accession

Primary (citable) accession number: Q83K38
Secondary accession number(s): Q7C0G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
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