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Protein

p-hydroxyphenylacetate 3-hydroxylase, oxygenase component

Gene

C2-hpah

Organism
Acinetobacter baumannii
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Oxygenase component of a two-component system that utilizes reduced FMN (FMNH2) supplied by the reductase component to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetate (3,4-DHPA). Also utilizes other reduced flavins such as FADH2 and reduced riboflavin to a lesser extent. Only the compounds with a hydroxyl group in the para (p-) position can be hydroxylated. May also oxidize phenol to catechol, and hydroxylate other phenol derivatives.6 Publications

Catalytic activityi

4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O.3 Publications

Enzyme regulationi

Inhibited by flavin concentrations greater than 15 µM. Also inhibited by excess p-hydroxyphenylacetate (HPA).3 Publications

Kineticsi

Km values measured using the C1-C2 complex. Kinetic parameters have been determined for recombinant and native enzyme in PubMed:15451173.

  1. KM=19 µM for 4-hydroxyphenylacetate (with FMN as cosubstrate)2 Publications
  2. KM=14 µM for 4-hydroxyphenylacetate (with FAD as cosubstrate)2 Publications

    pH dependencei

    Optimum pH is 6-10.1 Publication

    Pathwayi: 4-hydroxyphenylacetate degradation

    This protein is involved in step 1 of the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate.1 Publication
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. p-hydroxyphenylacetate 3-hydroxylase, oxygenase component (C2-hpah), p-hydroxyphenylacetate 3-hydroxylase, reductase component (C1-hpah)
    2. no protein annotated in this organism
    3. no protein annotated in this organism
    4. no protein annotated in this organism
    5. no protein annotated in this organism
    6. no protein annotated in this organism
    7. no protein annotated in this organism
    This subpathway is part of the pathway 4-hydroxyphenylacetate degradation, which is itself part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate, the pathway 4-hydroxyphenylacetate degradation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei112 – 1121FMN1 Publication
    Binding sitei120 – 1201Substrate
    Binding sitei146 – 1461Substrate
    Binding sitei292 – 2921FMN1 Publication
    Binding sitei296 – 2961FMN1 Publication
    Binding sitei296 – 2961Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi146 – 1483FMN1 Publication
    Nucleotide bindingi169 – 1713FMN1 Publication
    Nucleotide bindingi374 – 3752FMN1 Publication
    Nucleotide bindingi396 – 3972FMN1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi1.14.14.9. 98.
    UniPathwayiUPA00208; UER00416.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    p-hydroxyphenylacetate 3-hydroxylase, oxygenase component (EC:1.14.14.91 Publication)
    Alternative name(s):
    4-HPA 3-hydroxylaseBy similarity
    4-HPA 3-monooxygenase large componentBy similarity
    p-hydroxyphenylacetate 3-hydroxylase C2 component
    Gene namesi
    Name:C2-hpahImported
    OrganismiAcinetobacter baumannii
    Taxonomic identifieri470 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi120 – 1201H → D or N: Loss of hydroxylation activity. 7 to 10-fold higher rate constant for hydrogen peroxide elimination. 1 Publication
    Mutagenesisi120 – 1201H → K: 170-fold higher rate constant for hydrogen peroxide elimination. 1 Publication
    Mutagenesisi146 – 1461S → A: Decrease in rate constant for hydroxylation by 6-fold. 1 Publication
    Mutagenesisi146 – 1461S → C: Decrease in rate constant for hydroxylation by 45-fold and decreased enzymatic efficiency at pH greater than 9. 1 Publication
    Mutagenesisi171 – 1711S → A: Failure to form reaction intermediate; when associated with V-396. Decrease in rate constant for the formation of intermediate by 11-fold. Increase in rate constant for hydrogen peroxide elimination by 1400-fold. 1 Publication
    Mutagenesisi171 – 1711S → T: Increase in rate constant for hydrogen peroxide elimination by 8-fold. 1 Publication
    Mutagenesisi396 – 3961H → A: Decrease in rate constant for the formation of the reaction intermediate by 100-fold. Denatured above pH 10. 1 Publication
    Mutagenesisi396 – 3961H → K: Reduced binding with flavin. Lower rate constant. Denatured above pH 10. 1 Publication
    Mutagenesisi396 – 3961H → N: Decrease in rate constant for the formation of the reaction intermediate by 30-fold. Denatured above pH 10. 1 Publication
    Mutagenesisi396 – 3961H → R: Reduced binding with flavin. Lower rate constant. Denatured above pH 10. 1 Publication
    Mutagenesisi396 – 3961H → V: Failure to form reaction intermediate; when associated with A-171. Decrease in rate constant for the formation of the reaction intermediate by 300-fold. Denatured above pH 10. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422p-hydroxyphenylacetate 3-hydroxylase, oxygenase componentPRO_0000415755Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer. The p-hydroxyphenylacetate 3-hydroxylase (HpaH) is composed of an oxygenase component C2 and a reductase component C1.2 Publications

    Protein-protein interaction databases

    DIPiDIP-60804N.

    Structurei

    Secondary structure

    1
    422
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 293Combined sources
    Helixi40 – 5314Combined sources
    Helixi55 – 617Combined sources
    Helixi66 – 749Combined sources
    Helixi77 – 793Combined sources
    Beta strandi80 – 823Combined sources
    Helixi84 – 863Combined sources
    Helixi93 – 10614Combined sources
    Helixi108 – 12417Combined sources
    Helixi129 – 1368Combined sources
    Beta strandi144 – 1474Combined sources
    Beta strandi152 – 1576Combined sources
    Beta strandi160 – 17011Combined sources
    Helixi173 – 1753Combined sources
    Beta strandi177 – 18610Combined sources
    Beta strandi192 – 2009Combined sources
    Helixi201 – 2033Combined sources
    Beta strandi205 – 2073Combined sources
    Beta strandi212 – 2154Combined sources
    Helixi216 – 2183Combined sources
    Beta strandi221 – 23111Combined sources
    Helixi232 – 2343Combined sources
    Beta strandi235 – 2373Combined sources
    Helixi238 – 2425Combined sources
    Turni247 – 2504Combined sources
    Beta strandi256 – 2605Combined sources
    Helixi262 – 2665Combined sources
    Helixi269 – 28921Combined sources
    Turni295 – 2973Combined sources
    Helixi305 – 33733Combined sources
    Helixi344 – 36926Combined sources
    Helixi374 – 3774Combined sources
    Helixi382 – 39312Combined sources
    Turni397 – 3993Combined sources
    Helixi401 – 41212Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JBRX-ray2.30A/B/C/D1-422[»]
    2JBSX-ray2.80A/B/C/D1-422[»]
    2JBTX-ray2.80A/B/C/D1-422[»]
    ProteinModelPortaliQ6Q272.
    SMRiQ6Q272. Positions 23-422.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6Q272.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni263 – 2664Substrate binding

    Sequence similaritiesi

    Belongs to the HpaH/HsaA monooxygenase family.Curated

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    InterProiIPR013107. Acyl-CoA_DH_C_dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF08028. Acyl-CoA_dh_2. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q6Q272-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MENTVLNLDS DVIHACEAIF QPIRLVYTHA QTPDVSGVSM LEKIQQILPQ
    60 70 80 90 100
    IAKNAESAEQ LRRVPDENIK LLKEIGLHRA FQPKVYGGLE MSLPDFANCI
    110 120 130 140 150
    VTLAGACAGT AWAFSLLCTH SHQIAMFSKQ LQDEIWLKDP DATASSSIAP
    160 170 180 190 200
    FGKVEEVEGG IILNGDYGWS SGCDHAEYAI VGFNRFDADG NKIYSFGVIP
    210 220 230 240 250
    RSDYEIVDNW YAQAIKSSGS KMLKLVNVFI PEYRISKAKD MMEGKSAGFG
    260 270 280 290 300
    LYPDSKIFYT PYRPYFASGF SAVSLGIAER MIEAFKEKQR NRVRAYTGAN
    310 320 330 340 350
    VGLATPALMR IAESTHQVAA ARALLEKTWE DHRIHGLNHQ YPNKETLAFW
    360 370 380 390 400
    RTNQAYAVKM CIEAVDRLMA AAGATSFMDN SELQRLFRDA HMTGAHAYTD
    410 420
    YDVCAQILGR ELMGMEPDPT MV
    Length:422
    Mass (Da):46,950
    Last modified:July 5, 2004 - v1
    Checksum:i01BBA6D3C5CA5F80
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY566612 Genomic DNA. Translation: AAS75429.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY566612 Genomic DNA. Translation: AAS75429.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JBRX-ray2.30A/B/C/D1-422[»]
    2JBSX-ray2.80A/B/C/D1-422[»]
    2JBTX-ray2.80A/B/C/D1-422[»]
    ProteinModelPortaliQ6Q272.
    SMRiQ6Q272. Positions 23-422.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-60804N.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00208; UER00416.
    BRENDAi1.14.14.9. 98.

    Miscellaneous databases

    EvolutionaryTraceiQ6Q272.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    InterProiIPR013107. Acyl-CoA_DH_C_dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF08028. Acyl-CoA_dh_2. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHPAH_ACIBA
    AccessioniPrimary (citable) accession number: Q6Q272
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: July 5, 2004
    Last modified: November 11, 2015
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.