Q57160 (HPAB_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxyphenylacetate 3-monooxygenase oxygenase component
EC=1.14.14.9

Alternative name(s):
4-HPA 3-hydroxylase
4-HPA 3-monooxygenase large component

Gene names

Name:

hpaB

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Utilizes FADH2 supplied by hpaC or by another flavin reductase, to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-DHPA. Can also oxidize phenol to catechol, and hydroxylate other phenol derivatives. Ref.3
Catalytic activity	4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O.
Pathway	Aromatic compound metabolism; 4-hydroxyphenylacetate degradation; pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate: step 1/7.
Subunit structure	4-HPA 3-monooxygenase consists of a reductase component hpaC and an oxygenase component hpaB.
Induction	By 4-hydroxyphenylacetic acid.
Miscellaneous	E.coli K12 lacks the oxygenase component hpaB.
Sequence similarities	Belongs to the FADH(2)-utilizing monooxygenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	FAD
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	phenylacetate catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen 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 – 520	520	4-hydroxyphenylacetate 3-monooxygenase oxygenase component		PRO_0000084032

Sequences

	Sequence		Length	Mass (Da)
	Q57160 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 1E93BBCC29BBB55C	FASTA	520	58,848
	10 20 30 40 50 60 MKPEDFRAST QRPFTGEEYL KSLQDGREIY IYGERVKDVT THPAFRNAAA SVAQLYDALH 70 80 90 100 110 120 KPEMQDSLCW NTDTGSGGYT HKFFRVAKSA DDLRHERDAI AEWSRLSYGW MGRTPDYKAA 130 140 150 160 170 180 FGCALGGTPG FYGQFEQNAR NWYTRIQETG LYFNHAIVNP PIDRHLPTDK VKDVYIKLEK 190 200 210 220 230 240 ETDAGIIVSG AKVVATNSAL THYNMIGFGS AQVMGENPDF ALMFVAPMDA DGVKLISRAS 250 260 270 280 290 300 YEMVAGATGS PYDYPLSSRF DENDAILVMD NVLIPWENVL LYRDFDRCRR WTMEGGFARM 310 320 330 340 350 360 YPLQACVRLA VKLDFITALL KKSLECTGTL EFRGVQADLG EVVAWRNTFW ALSDSMCSEA 370 380 390 400 410 420 TPWVNGAYLP DHAALQTYRV LAPMAYAKIK NIIERNVTSG LIYLPSSARD LNNPQIDQYL 430 440 450 460 470 480 AKYVRGSNGM DHVQRIKILK LMWDAIGSEF GGRHELYEIN YSGSQDEIRL QCLRQAQSSG 490 500 510 520 NMDKMMAMVD RCLSEYDQNG WTVPHLHNND DINMLDKLLK

References

[1]	"Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme." Prieto M.A., Garcia J.L. J. Biol. Chem. 269:22823-22829(1994) [PubMed: 8077235] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20. Strain: W / ATCC 11105 / DSM 1900.
[2]	"Molecular characterization of the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli W: engineering a mobile aromatic degradative cluster." Prieto M.A., Diaz E., Garcia J.L. J. Bacteriol. 178:111-120(1996) [PubMed: 8550403] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: W / ATCC 11105 / DSM 1900.
[3]	"Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase." Xun L., Sandvik E.R. Appl. Environ. Microbiol. 66:481-486(2000) [PubMed: 10653707] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z37980 Genomic DNA. Translation: CAA86048.1. Z29081 Genomic DNA. Translation: CAA82321.1.
PIR	B55349.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-2841.
Family and domain databases
InterPro	IPR006091. Acyl-CoA_Oxase/DH_cen-dom. IPR009075. AcylCo_DH/oxidase_C. IPR009100. AcylCoA_DH/oxidase. IPR024677. HpaB/PvcC. IPR004925. HpaB/PvcC/4-BUDH. IPR024719. HpaB/PvcC/4-BUDH_C. IPR024674. HpaB/PvcC/4-BUDH_N. IPR012688. HpaB_gammaproteobact. [Graphical view]
Gene3D	G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
Pfam	PF03241. HpaB. 1 hit. PF11794. HpaB_N. 1 hit. [Graphical view]
PIRSF	PIRSF500125. 4_HPA_large. 1 hit. PIRSF000331. HpaA_HpaB. 1 hit.
SUPFAM	SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 1 hit.
TIGRFAMs	TIGR02310. HpaB-2. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HPAB_ECOLX

Accession

Primary (citable) accession number: Q57160

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program