Reviewed, UniProtKB/Swiss-Prot Q0T1X7 (HCAD_SHIF8)

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:	SFV_2590

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	410 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, 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.
Catalytic activity	Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH. HAMAP MF_01651
Cofactor	FAD By similarity.
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.
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 electron carrier activity 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 – 410	410	3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component HAMAP MF_01651		PRO_0000333728
Regions
	Nucleotide binding	5 – 36	32	FAD Potential
	Nucleotide binding	146 – 184	39	NAD Potential

Sequences

	Sequence		Length	Mass (Da)
	Q0T1X7-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 69DC1B6419C30C19	FASTA	410	44,972
	10 20 30 40 50 60 MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS MLLEDSPQLQ 70 80 90 100 110 120 QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH WDQLFIATGA AARPLPLLDA 130 140 150 160 170 180 LGERCFTLHH AGDAARLREV LQPERSVVIV GAGTIGLELA ASATQRSAAQ RSAAQRRCKV 190 200 210 220 230 240 TVIELAATVM GRNAPPPVQR YLLQRHQQAG VRILLNNAIE HVVDGEKVEL TLQSGETLQA 250 260 270 280 290 300 DVVIYGIGIS ANEQLAREAN LDTANGIVID EACRTCDPAI FAGGDVAITR LDNGALHRCE 310 320 330 340 350 360 SWENANNQAQ IAAAAMLGLP LPLLPPPWFW SDQYSDNLQF IGDMRGDDWL CRGNPETQKA 370 380 390 400 410 IWFNLQNGVL IGAVTLNQGR EIRPIRKWIQ SGKTFDAKLL IDENIALKSL

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: ABF04688.1.
RefSeq	YP_689993.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0T1X7.
Genome annotation databases
GeneID	4210038.
GenomeReviews	Gene locus SFV_2590 in contig CP000266_GR.
KEGG	sfv:SFV_2590.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0T1X7.
OMA	HAPYERP.
Enzyme and pathway databases
BioCyc	SFLE373384:SFV_2590-MON.
Family and domain databases
HAMAP	MF_01651. [Tree]
InterPro	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.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

HCAD_SHIF8

Accession

Primary (citable) accession number: Q0T1X7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 5, 2006
Last modified:	November 3, 2009
This is version 29 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)