B1IVT5 (HCAD_ECOLC) Reviewed, UniProtKB/Swiss-Prot

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:	EcolC_1135

Organism

Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) [Complete proteome] [HAMAP]

Taxonomic identifier

481805 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli › Escherichia coli C

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-Rule MF_01651
Catalytic activity	Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH. HAMAP-Rule MF_01651
Cofactor	FAD By similarity. HAMAP-Rule MF_01651
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule 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	3-phenylpropionate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	3-phenylpropionate dioxygenase activity Inferred from electronic annotation. Source: HAMAP ferredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
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-Rule MF_01651		PRO_1000186985
Regions
	Nucleotide binding	5 – 36	32	FAD Potential
	Nucleotide binding	146 – 174	29	NAD Potential

Sequences

	Sequence		Length	Mass (Da)
	B1IVT5 [UniParc]. Last modified April 29, 2008. Version 1. Checksum: F5A1A06C4F1DFF36	FASTA	400	43,978
	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 LQPERSVVII 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]

"Complete sequence of Escherichia coli C str. ATCC 8739." Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Mikhailova N., Ingram L., Richardson P. Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8739 / DSM 1576 / Crooks.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000946 Genomic DNA. Translation: ACA76802.1.
RefSeq	YP_001724129.1. NC_010468.1.
3D structure databases
ProteinModelPortal	B1IVT5.
SMR	B1IVT5. Positions 5-386.
ModBase	Search...
Protein-protein interaction databases
STRING	481805.EcolC_1135.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACA76802; ACA76802; EcolC_1135.
GeneID	6068037.
KEGG	ecl:EcolC_1135.
PATRIC	18224941. VBIEscCol82905_1212.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0446.
HOGENOM	HOG000276711.
KO	K00529.
OMA	LETDMLL.
ProtClustDB	PRK09754.
Enzyme and pathway databases
BioCyc	ECOL481805:GI3G-1166-MONOMER.
UniPathway	UPA00714.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
HAMAP	MF_01651. HcaD.
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR023744. HcaD. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HCAD_ECOLC

Accession

Primary (citable) accession number: B1IVT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	April 29, 2008
Last modified:	May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program