P77650 (HCAD_ECOLI) 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
Synonyms:	hcaA4, phdA, yfhY
Ordered Locus Names:	b2542, JW2526

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. HAMAP-Rule MF_01651
Catalytic activity	Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH. HAMAP-Rule MF_01651
Cofactor	FAD.
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).
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 Reference proteome
Gene Ontology (GO)
Biological_process	3-phenylpropionate catabolic process Inferred from mutant phenotype PubMed 3531186. Source: EcoCyc 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_0000167661
Regions
	Nucleotide binding	5 – 36	32	FAD Potential
	Nucleotide binding	146 – 174	29	NAD Potential

Sequences

	Sequence		Length	Mass (Da)
	P77650 [UniParc]. Last modified February 1, 1997. 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12." Diaz E., Ferrandez A., Garcia J.L. J. Bacteriol. 180:2915-2923(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11070 Genomic DNA. Translation: CAA71952.1. U00096 Genomic DNA. Translation: AAC75595.1. AP009048 Genomic DNA. Translation: BAA16445.1.
PIR	E65031.
RefSeq	NP_417037.1. NC_000913.2. YP_490770.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P77650.
SMR	P77650. Positions 5-386.
ModBase	Search...
Protein-protein interaction databases
IntAct	P77650. 2 interactions.
STRING	511145.b2542.
PTM databases
PhosSite	P0809399.
Proteomic databases
PaxDb	P77650.
PRIDE	P77650.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75595; AAC75595; b2542. BAA16445; BAA16445; BAA16445.
GeneID	12930468. 945427.
KEGG	ecj:Y75_p2495. eco:b2542.
PATRIC	32120481. VBIEscCol129921_2643.
Organism-specific databases
EchoBASE	EB3233.
EcoGene	EG13460. hcaD.
Phylogenomic databases
eggNOG	COG0446.
HOGENOM	HOG000276711.
KO	K00529.
OMA	LETDMLL.
ProtClustDB	PRK09754.
Enzyme and pathway databases
BioCyc	EcoCyc:HCAD-MONOMER. ECOL316407:JW2526-MONOMER. MetaCyc:HCAD-MONOMER.
UniPathway	UPA00714.
Gene expression databases
Genevestigator	P77650.
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_ECOLI

Accession

Primary (citable) accession number: P77650
Secondary accession number(s): O08100

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program