Reviewed, UniProtKB/Swiss-Prot Q3YZ11 (HCAD_SHISS)

Names and origin

Protein names

Recommended name:
    3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component
    EC=1.18.1.3
Alternative name(s):
    Digoxigenin system ferredoxin--NAD(+) reductase component

Gene names

Name:	hcaD
Ordered Locus Names:	SSON_2624

Organism

Shigella sonnei (strain Ss046) [Complete proteome] [HAMAP]

Taxonomic identifier

300269 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Part of the multicomponent 3-phenylpropionate dioxygenase, that 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_01651
Catalytic activity	Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH. HAMAP MF_01651
Cofactor	FAD By similarity. HAMAP MF_01651
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01651
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_01651
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	FAD Flavoprotein NAD
Molecular function	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	3-phenylpropionate dioxygenase activity Inferred from electronic annotation. Source: HAMAP FAD binding Inferred from electronic annotation. Source: InterPro ferredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 400	400	3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component HAMAP MF_01651		PRO_0000333729
Regions
	Nucleotide binding	5 – 36	32	FAD Potential
	Nucleotide binding	146 – 174	29	NAD Potential

Sequences

	Sequence		Length	Mass (Da)
	Q3YZ11-1 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: D7AD540F7B75272F	FASTA	400	43,976
	10 20 30 40 50 60 MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS MLLEDSPQLQ 70 80 90 100 110 120 QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH WDQLFIAIGA AARPLPLLDA 130 140 150 160 170 180 LGERCFTLRH AGDAARLREV LQPERSVVIV GAGTIGLELA ASATQRRCKV TVIELAATVM 190 200 210 220 230 240 GRNAPPPVQR YLLQRHQQAG VRILLNNAIE HVVDGEKVEL TLQSGETLQA DVVIYGIGIS 250 260 270 280 290 300 ANEQLAREAN LDTANGIVID EACRTCDPAI FAGGDVAITR LDNGALHRCE SWENANNQAQ 310 320 330 340 350 360 IAAAAMLGLP LPLLPPPWFW SDQYSDNLQF IGDMRGDDWL CRGNPETQKA IWFNLQNGVL 370 380 390 400 IGAVTLNQGR EIRPIRKWIQ SGKTFDAKLL IDENIALKSL

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: 16275786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000038 Genomic DNA. Translation: AAZ89251.1.
RefSeq	YP_311486.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q3YZ11.
Genome annotation databases
GeneID	3668244.
GenomeReviews	Gene locus SSON_2624 in contig CP000038_GR.
KEGG	ssn:SSON_2624.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0446.
HOGENOM	HBG644911.
OMA	SATQRGC.
Enzyme and pathway databases
BioCyc	SSON300269:SSO_2624-MONOMER.
Family and domain databases
HAMAP	MF_01651. HcaD. [Tree]
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
ProtoNet	Search...

Entry information

Entry name

HCAD_SHISS

Accession

Primary (citable) accession number: Q3YZ11

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 27, 2005
Last modified:	February 9, 2010
This is version 46 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)