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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)DescriptionActionsGraphical viewLength
    Binding sitei112FMN1 Publication1
    Binding sitei120Substrate1
    Binding sitei146Substrate1
    Binding sitei292FMN1 Publication1
    Binding sitei296FMN1 Publication1
    Binding sitei296Substrate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi146 – 148FMN1 Publication3
    Nucleotide bindingi169 – 171FMN1 Publication3
    Nucleotide bindingi374 – 375FMN1 Publication2
    Nucleotide bindingi396 – 397FMN1 Publication2

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi120H → D or N: Loss of hydroxylation activity. 7 to 10-fold higher rate constant for hydrogen peroxide elimination. 1 Publication1
    Mutagenesisi120H → K: 170-fold higher rate constant for hydrogen peroxide elimination. 1 Publication1
    Mutagenesisi146S → A: Decrease in rate constant for hydroxylation by 6-fold. 1 Publication1
    Mutagenesisi146S → C: Decrease in rate constant for hydroxylation by 45-fold and decreased enzymatic efficiency at pH greater than 9. 1 Publication1
    Mutagenesisi171S → 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 Publication1
    Mutagenesisi171S → T: Increase in rate constant for hydrogen peroxide elimination by 8-fold. 1 Publication1
    Mutagenesisi396H → A: Decrease in rate constant for the formation of the reaction intermediate by 100-fold. Denatured above pH 10. 1 Publication1
    Mutagenesisi396H → K: Reduced binding with flavin. Lower rate constant. Denatured above pH 10. 1 Publication1
    Mutagenesisi396H → N: Decrease in rate constant for the formation of the reaction intermediate by 30-fold. Denatured above pH 10. 1 Publication1
    Mutagenesisi396H → R: Reduced binding with flavin. Lower rate constant. Denatured above pH 10. 1 Publication1
    Mutagenesisi396H → 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 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004157551 – 422p-hydroxyphenylacetate 3-hydroxylase, oxygenase componentAdd BLAST422

    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

    1422
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi27 – 29Combined sources3
    Helixi40 – 53Combined sources14
    Helixi55 – 61Combined sources7
    Helixi66 – 74Combined sources9
    Helixi77 – 79Combined sources3
    Beta strandi80 – 82Combined sources3
    Helixi84 – 86Combined sources3
    Helixi93 – 106Combined sources14
    Helixi108 – 124Combined sources17
    Helixi129 – 136Combined sources8
    Beta strandi144 – 147Combined sources4
    Beta strandi152 – 157Combined sources6
    Beta strandi160 – 170Combined sources11
    Helixi173 – 175Combined sources3
    Beta strandi177 – 186Combined sources10
    Beta strandi192 – 200Combined sources9
    Helixi201 – 203Combined sources3
    Beta strandi205 – 207Combined sources3
    Beta strandi212 – 215Combined sources4
    Helixi216 – 218Combined sources3
    Beta strandi221 – 231Combined sources11
    Helixi232 – 234Combined sources3
    Beta strandi235 – 237Combined sources3
    Helixi238 – 242Combined sources5
    Turni247 – 250Combined sources4
    Beta strandi256 – 260Combined sources5
    Helixi262 – 266Combined sources5
    Helixi269 – 289Combined sources21
    Turni295 – 297Combined sources3
    Helixi305 – 337Combined sources33
    Helixi344 – 369Combined sources26
    Helixi374 – 377Combined sources4
    Helixi382 – 393Combined sources12
    Turni397 – 399Combined sources3
    Helixi401 – 412Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6Q272.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni263 – 266Substrate binding4

    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
    PDB 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.
    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 2, 2016
    This is version 61 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.