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Q57160 (HPAB_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.3

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5205204-hydroxyphenylacetate 3-monooxygenase oxygenase component
PRO_0000084032

Sequences

Sequence LengthMass (Da)Tools
Q57160 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1E93BBCC29BBB55C

FASTA52058,848
        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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
PIRB55349.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-2841.
UniPathwayUPA00208; UER00416.

Family and domain databases

Gene3D2.40.110.10. 1 hit.
InterProIPR006091. 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]
PfamPF03241. HpaB. 1 hit.
PF11794. HpaB_N. 1 hit.
[Graphical view]
PIRSFPIRSF500125. 4_HPA_large. 1 hit.
PIRSF000331. HpaA_HpaB. 1 hit.
SUPFAMSSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 1 hit.
TIGRFAMsTIGR02310. HpaB-2. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHPAB_ECOLX
AccessionPrimary (citable) accession number: Q57160
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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