Reviewed, UniProtKB/Swiss-Prot A7ZPY5 (HCAD_ECO24)

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:	EcE24377A_2827

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	400 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 cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
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 – 400	400	3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component HAMAP MF_01651		PRO_0000333724
Regions
	Nucleotide binding	5 – 36	32	FAD Potential
	Nucleotide binding	146 – 174	29	NAD Potential

Sequences

	Sequence		Length	Mass (Da)
	A7ZPY5-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 281F7C3E44173AAE	FASTA	400	44,008
	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 LGERCFTLRH AGDAARLREV LQPERSVVIV GAGTIGLELA ASATQRRCKV TVIELAATVM 190 200 210 220 230 240 GRNAPLPVQR YLLQRHQQAG VRILLNNAIE HVVDGEKVEL TLQSGETLQA DVVIYGIGIS 250 260 270 280 290 300 ANEQLAREAN LDTANGIVID EVCRTCDPAI 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]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000800 Genomic DNA. Translation: ABV18229.1.
RefSeq	YP_001463864.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZPY5.
Genome annotation databases
GeneID	5589044.
GenomeReviews	Gene locus EcE24377A_2827 in contig CP000800_GR.
KEGG	ecw:EcE24377A_2827.
NMPDR	fig|331111.3.peg.556.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	SATIENX.
Family and domain databases
HAMAP	MF_01651. [Tree]
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
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_ECO24

Accession

Primary (citable) accession number: A7ZPY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	October 23, 2007
Last modified:	November 3, 2009
This is version 22 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)