P77397 (MHPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase
Short name=3-HCI hydroxylase
Short name=3-HPP hydroxylase
EC=1.14.13.127

Gene names

Name:	mhpA
Ordered Locus Names:	b0347, JW0338

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	554 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI). Ref.6
Catalytic activity	3-(3-hydroxyphenyl)propanoate + NADH + O2 = 3-(2,3-dihydroxyphenyl)propanoate + H2O + NAD+. HAMAP-Rule MF_01652 (2E)-3-(3-hydroxyphenyl)prop-2-enoate + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + H2O + NAD+. HAMAP-Rule MF_01652
Cofactor	FAD By similarity. HAMAP-Rule MF_01652
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01652
Sequence similarities	Belongs to the PheA/TfdB FAD monooxygenase 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-(3-hydroxy)phenylpropionate catabolic process Inferred from electronic annotation. Source: HAMAP 3-phenylpropionate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway phenylpropanoid catabolic process Inferred from mutant phenotype PubMed 3531186. Source: EcoCyc
Molecular_function	3-(3-hydroxyphenyl)propionate hydroxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 554	554	3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase HAMAP-Rule MF_01652		PRO_0000214043
Regions
	Nucleotide binding	17 – 46	30	FAD Potential
	Nucleotide binding	285 – 295	11	FAD Potential
Experimental info
	Sequence conflict	272	1	Q → H in BAA13052. Ref.1
	Sequence conflict	360	1	L → P in BAA13052. Ref.1
	Sequence conflict	502	1	W → G in BAA13052. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P77397 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 1D56CB799E9F8A8E	FASTA	554	62,186
	10 20 30 40 50 60 MAIQHPDIQP AVNHSVQVAI AGAGPVGLMM ANYLGQMGID VLVVEKLDKL IDYPRAIGID 70 80 90 100 110 120 DEALRTMQSV GLVDDVLPHT TPWHAMRFLT PKGRCFADIQ PMTDEFGWPR RNAFIQPQVD 130 140 150 160 170 180 AVMLEGVSRF PNVRCLFSRE LEAFSQQDDE VTLHLKTAEG QREIVKAQWL VACDGGASFV 190 200 210 220 230 240 RRTLNVPFEG KTAPNQWIVV DIANDPLSTP HIYLCCDPVR PYVSAALPHA VRRFEFMVMP 250 260 270 280 290 300 GETEEQLREP QNMRKLLSKV LPNPDNVELI RQRVYTHNAR LAQRFRIDRV LLAGDAAHIM 310 320 330 340 350 360 PVWQGQGYNS GMRDAFNLAW KLALVIQGKA RDALLDTYQQ ERRDHAKAMI DLSVTAGNVL 370 380 390 400 410 420 APPKRWQGTL RDGVSWLLNY LPPVKRYFLE MRFKPMPQYY GGALMREGEA KHSPVGKMFI 430 440 450 460 470 480 QPKVTLENGD VTLLDNAIGA NFAVIGWGCN PLWGMSDEQI QQWRALGTRF IQVVPEVQIH 490 500 510 520 530 540 TAQDNHDGVL RVGDTQGRLR SWFAQHNASL VVMRPDRFVA ATAIPQTLGK TLNKLASVMT 550 LTRPDADVSV EKVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Kawamukai M. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12." Ferrandez A., Garcia J.L., Diaz E. J. Bacteriol. 179:2573-2581(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / CS520.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	"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.
[6]	"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: FUNCTION IN CATABOLISM OF 3-HYDROXY DERIVATIVES OF PHENYLPROPIONIC ACID.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D86239 Genomic DNA. Translation: BAA13052.1. Y09555 Genomic DNA. Translation: CAA70747.1. U73857 Genomic DNA. Translation: AAB18071.1. U00096 Genomic DNA. Translation: AAC73450.1. AP009048 Genomic DNA. Translation: BAE76129.1.
PIR	C64762.
RefSeq	NP_414881.1. NC_000913.2. YP_488641.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P77397.
SMR	P77397. Positions 17-419.
ModBase	Search...
Protein-protein interaction databases
IntAct	P77397. 2 interactions.
STRING	511145.b0347.
Proteomic databases
PaxDb	P77397.
PRIDE	P77397.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73450; AAC73450; b0347. BAE76129; BAE76129; BAE76129.
GeneID	12931734. 945197.
KEGG	ecj:Y75_p0336. eco:b0347.
PATRIC	32115827. VBIEscCol129921_0355.
Organism-specific databases
EchoBASE	EB4166.
EcoGene	EG20273. mhpA.
Phylogenomic databases
eggNOG	COG0654.
HOGENOM	HOG000221401.
KO	K05712.
OMA	RIAGSFR.
ProtClustDB	PRK06183.
Enzyme and pathway databases
BioCyc	EcoCyc:MHPHYDROXY-MONOMER. ECOL316407:JW0338-MONOMER. MetaCyc:MHPHYDROXY-MONOMER.
UniPathway	UPA00714.
Gene expression databases
Genevestigator	P77397.
Family and domain databases
HAMAP	MF_01652. MhpA.
InterPro	IPR023786. 3-HPP/3HCI_hydroxylase. IPR002938. mOase_FAD-bd. IPR003042. Rng_hydrolase-like. [Graphical view]
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...

Entry information

Entry name

MHPA_ECOLI

Accession

Primary (citable) accession number: P77397
Secondary accession number(s): P71203, P77047, Q2MC77

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program