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P00437

- PCXB_PSEPU

UniProt

P00437 - PCXB_PSEPU

Protein

Protocatechuate 3,4-dioxygenase beta chain

Gene

pcaH

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.

    Catalytic activityi

    3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate.

    Cofactori

    Binds Fe3+ ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi109 – 1091Iron; catalytic1 Publication
    Metal bindingi148 – 1481Iron; catalytic1 Publication
    Metal bindingi161 – 1611Iron; catalytic1 Publication
    Metal bindingi163 – 1631Iron; catalytic1 Publication

    GO - Molecular functioni

    1. ferric iron binding Source: InterPro
    2. protocatechuate 3,4-dioxygenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. beta-ketoadipate pathway Source: UniProtKB-UniPathway
    2. protocatechuate catabolic process Source: InterPro

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3185.
    RETL1328306-WGS:GSTH-5905-MONOMER.
    UniPathwayiUPA00157; UER00264.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protocatechuate 3,4-dioxygenase beta chain (EC:1.13.11.3)
    Alternative name(s):
    3,4-PCD
    Gene namesi
    Name:pcaH
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 239238Protocatechuate 3,4-dioxygenase beta chainPRO_0000085098Add
    BLAST

    Interactioni

    Subunit structurei

    The enzyme is an oligomer of 12 copies of the alpha and beta chains.

    Protein-protein interaction databases

    IntActiP00437. 1 interaction.

    Structurei

    Secondary structure

    1
    239
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93
    Turni14 – 163
    Helixi26 – 283
    Turni29 – 313
    Helixi44 – 474
    Turni59 – 624
    Turni64 – 685
    Beta strandi70 – 723
    Beta strandi78 – 8710
    Beta strandi97 – 1015
    Beta strandi127 – 1315
    Beta strandi136 – 1438
    Beta strandi148 – 1536
    Beta strandi156 – 1583
    Beta strandi160 – 1667
    Turni171 – 1733
    Beta strandi175 – 1817
    Helixi187 – 1893
    Helixi193 – 1953
    Helixi199 – 2035
    Beta strandi206 – 2094
    Helixi211 – 2133
    Turni216 – 2183
    Beta strandi219 – 2235
    Beta strandi226 – 2283
    Beta strandi231 – 2333

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YKKX-ray2.06B/D/F/H/J/L2-239[»]
    1YKLX-ray2.25B/D/F/H/J/L2-239[»]
    1YKMX-ray2.22B/D/F/H/J/L2-239[»]
    1YKNX-ray2.06B/D/F/H/J/L2-239[»]
    1YKOX-ray2.54B/D/F/H/J/L2-239[»]
    1YKPX-ray2.41B/D/F/H/J/L2-239[»]
    2PCDX-ray2.15M/N/O/P/Q/R2-239[»]
    3LKTX-ray1.65M/N/O/P/Q/R2-239[»]
    3LMXX-ray2.20M/N/O2-239[»]
    3LXVX-ray1.90M/N/O2-239[»]
    3MFLX-ray1.78M/N/O2-239[»]
    3MI1X-ray1.74M/N/O2-239[»]
    3MI5X-ray1.78M/N/O/P/Q/R2-239[»]
    3MV4X-ray1.59M/N/O2-239[»]
    3MV6X-ray1.86M/N/O2-239[»]
    3PCAX-ray2.20M/N/O/P/Q/R2-239[»]
    3PCBX-ray2.19M/N/O/P/Q/R2-239[»]
    3PCCX-ray1.98M/N/O/P/Q/R2-239[»]
    3PCDX-ray2.10M/N/O/P/Q/R2-239[»]
    3PCEX-ray2.06M/N/O/P/Q/R2-239[»]
    3PCFX-ray2.15M/N/O/P/Q/R2-239[»]
    3PCGX-ray1.96M/N/O/P/Q/R2-239[»]
    3PCHX-ray2.05M/N/O/P/Q/R2-239[»]
    3PCIX-ray2.21M/N/O/P/Q/R2-239[»]
    3PCJX-ray2.13M/N/O/P/Q/R2-239[»]
    3PCKX-ray2.13M/N/O/P/Q/R2-239[»]
    3PCLX-ray2.15M/N/O/P/Q/R2-239[»]
    3PCMX-ray2.25M/N/O/P/Q/R2-239[»]
    3PCNX-ray2.40M/N/O/P/Q/R2-239[»]
    3T63X-ray1.54M/N/O2-239[»]
    3T67X-ray1.67M/N/O2-239[»]
    ProteinModelPortaliP00437.
    SMRiP00437. Positions 2-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00437.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di2.60.130.10. 1 hit.
    InterProiIPR000627. Intradiol_dOase_C.
    IPR015889. Intradiol_dOase_core.
    IPR024756. PCDO_beta_N.
    IPR012785. Protocat_dOase_b.
    [Graphical view]
    PfamiPF00775. Dioxygenase_C. 1 hit.
    PF12391. PCDO_beta_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF49482. SSF49482. 1 hit.
    TIGRFAMsiTIGR02422. protocat_beta. 1 hit.
    PROSITEiPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00437-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAQDNSRFV IRDRNWHPKA LTPDYKTSIA RSPRQALVSI PQSISETTGP    50
    NFSHLGFGAH DHDLLLNFNN GGLPIGERII VAGRVVDQYG KPVPNTLVEM 100
    WQANAGGRYR HKNDRYLAPL DPNFGGVGRC LTDSDGYYSF RTIKPGPYPW 150
    RNGPNDWRPA HIHFGISGPS IATKLITQLY FEGDPLIPMC PIVKSIANPE 200
    AVQQLIAKLD MNNANPMDCL AYRFDIVLRG QRKTHFENC 239
    Length:239
    Mass (Da):26,793
    Last modified:January 23, 2007 - v3
    Checksum:i8F8CC293B6E434CE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti62 – 621H → D AA sequence (PubMed:115853)Curated
    Sequence conflicti70 – 701N → D AA sequence (PubMed:115853)Curated
    Sequence conflicti72 – 721Missing AA sequence (PubMed:115853)Curated
    Sequence conflicti218 – 2181D → N AA sequence (PubMed:115853)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14836 Genomic DNA. Translation: AAB41024.1.
    PIRiA36930. DAPSBA.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14836 Genomic DNA. Translation: AAB41024.1 .
    PIRi A36930. DAPSBA.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YKK X-ray 2.06 B/D/F/H/J/L 2-239 [» ]
    1YKL X-ray 2.25 B/D/F/H/J/L 2-239 [» ]
    1YKM X-ray 2.22 B/D/F/H/J/L 2-239 [» ]
    1YKN X-ray 2.06 B/D/F/H/J/L 2-239 [» ]
    1YKO X-ray 2.54 B/D/F/H/J/L 2-239 [» ]
    1YKP X-ray 2.41 B/D/F/H/J/L 2-239 [» ]
    2PCD X-ray 2.15 M/N/O/P/Q/R 2-239 [» ]
    3LKT X-ray 1.65 M/N/O/P/Q/R 2-239 [» ]
    3LMX X-ray 2.20 M/N/O 2-239 [» ]
    3LXV X-ray 1.90 M/N/O 2-239 [» ]
    3MFL X-ray 1.78 M/N/O 2-239 [» ]
    3MI1 X-ray 1.74 M/N/O 2-239 [» ]
    3MI5 X-ray 1.78 M/N/O/P/Q/R 2-239 [» ]
    3MV4 X-ray 1.59 M/N/O 2-239 [» ]
    3MV6 X-ray 1.86 M/N/O 2-239 [» ]
    3PCA X-ray 2.20 M/N/O/P/Q/R 2-239 [» ]
    3PCB X-ray 2.19 M/N/O/P/Q/R 2-239 [» ]
    3PCC X-ray 1.98 M/N/O/P/Q/R 2-239 [» ]
    3PCD X-ray 2.10 M/N/O/P/Q/R 2-239 [» ]
    3PCE X-ray 2.06 M/N/O/P/Q/R 2-239 [» ]
    3PCF X-ray 2.15 M/N/O/P/Q/R 2-239 [» ]
    3PCG X-ray 1.96 M/N/O/P/Q/R 2-239 [» ]
    3PCH X-ray 2.05 M/N/O/P/Q/R 2-239 [» ]
    3PCI X-ray 2.21 M/N/O/P/Q/R 2-239 [» ]
    3PCJ X-ray 2.13 M/N/O/P/Q/R 2-239 [» ]
    3PCK X-ray 2.13 M/N/O/P/Q/R 2-239 [» ]
    3PCL X-ray 2.15 M/N/O/P/Q/R 2-239 [» ]
    3PCM X-ray 2.25 M/N/O/P/Q/R 2-239 [» ]
    3PCN X-ray 2.40 M/N/O/P/Q/R 2-239 [» ]
    3T63 X-ray 1.54 M/N/O 2-239 [» ]
    3T67 X-ray 1.67 M/N/O 2-239 [» ]
    ProteinModelPortali P00437.
    SMRi P00437. Positions 2-239.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00437. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00157 ; UER00264 .
    BioCyci MetaCyc:MONOMER-3185.
    RETL1328306-WGS:GSTH-5905-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P00437.

    Family and domain databases

    Gene3Di 2.60.130.10. 1 hit.
    InterProi IPR000627. Intradiol_dOase_C.
    IPR015889. Intradiol_dOase_core.
    IPR024756. PCDO_beta_N.
    IPR012785. Protocat_dOase_b.
    [Graphical view ]
    Pfami PF00775. Dioxygenase_C. 1 hit.
    PF12391. PCDO_beta_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49482. SSF49482. 1 hit.
    TIGRFAMsi TIGR02422. protocat_beta. 1 hit.
    PROSITEi PS00083. INTRADIOL_DIOXYGENAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes."
      Frazee R.W., Livingston D.M., Laporte D.C., Lipscomb J.D.
      J. Bacteriol. 175:6194-6202(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
    2. "The complete amino acid sequence of the beta-subunit of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa."
      Iwaki M., Kagamiyama H., Nozaki M.
      J. Biochem. 86:1159-1162(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-239.
    3. "Structure and assembly of protocatechuate 3,4-dioxygenase."
      Ohlendorf D.H., Lipscomb J.D., Weber P.C.
      Nature 336:403-405(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    4. "Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15-A resolution."
      Ohlendorf D.H., Orville A.M., Lipscomb J.D.
      J. Mol. Biol. 244:586-608(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
      Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
    5. "Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site."
      Orville A.M., Elango N., Lipscomb J.D., Ohlendorf D.H.
      Biochemistry 36:10039-10051(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
      Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
    6. "Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding."
      Orville A.M., Lipscomb J.D., Ohlendorf D.H.
      Biochemistry 36:10052-10066(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS).
      Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
    7. "Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate."
      Elgren T.E., Orville A.M., Kelly K.A., Lipscomb J.D., Ohlendorf D.H., Que L. Jr.
      Biochemistry 36:11504-11513(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
      Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.

    Entry informationi

    Entry nameiPCXB_PSEPU
    AccessioniPrimary (citable) accession number: P00437
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Strain ATCC 23975 was originally classified as being from Pseudomonas aeruginosa.Curated

    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

    External Data

    Dasty 3