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P00436

- PCXA_PSEPU

UniProt

P00436 - PCXA_PSEPU

Protein

Protocatechuate 3,4-dioxygenase alpha chain

Gene

pcaG

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 99 (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
    Binding sitei134 – 1341ProtocatechuateSequence Analysis

    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

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    Iron

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3186.
    RETL1328306-WGS:GSTH-5904-MONOMER.
    UniPathwayiUPA00157; UER00264.

    Names & Taxonomyi

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 201200Protocatechuate 3,4-dioxygenase alpha chainPRO_0000085095Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiP00436. 1 interaction.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 225
    Turni24 – 285
    Beta strandi45 – 473
    Beta strandi49 – 546
    Beta strandi68 – 725
    Beta strandi88 – 903
    Beta strandi92 – 976
    Turni100 – 1023
    Beta strandi104 – 1107
    Beta strandi127 – 1326
    Beta strandi140 – 1467
    Helixi147 – 1493
    Helixi150 – 1545
    Helixi159 – 1613
    Beta strandi162 – 1643
    Helixi165 – 1684
    Helixi169 – 1713
    Beta strandi172 – 1787
    Beta strandi181 – 1855

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YKKX-ray2.06A/C/E/G/I/K2-201[»]
    1YKLX-ray2.25A/C/E/G/I/K2-201[»]
    1YKMX-ray2.22A/C/E/G/I/K2-201[»]
    1YKNX-ray2.06A/C/E/G/I/K2-201[»]
    1YKOX-ray2.54A/C/E/G/I/K2-201[»]
    1YKPX-ray2.41A/C/E/G/I/K2-201[»]
    2PCDX-ray2.15A/B/C/D/E/F2-201[»]
    3LKTX-ray1.65A/B/C/D/E/F2-201[»]
    3LMXX-ray2.20A/B/C2-201[»]
    3LXVX-ray1.90A/B/C2-201[»]
    3MFLX-ray1.78A/B/C2-201[»]
    3MI1X-ray1.74A/B/C2-201[»]
    3MI5X-ray1.78A/B/C/D/E/F2-201[»]
    3MV4X-ray1.59A/B/C2-201[»]
    3MV6X-ray1.86A/B/C2-201[»]
    3PCAX-ray2.20A/B/C/D/E/F2-201[»]
    3PCBX-ray2.19A/B/C/D/E/F2-201[»]
    3PCCX-ray1.98A/B/C/D/E/F2-201[»]
    3PCDX-ray2.10A/B/C/D/E/F2-201[»]
    3PCEX-ray2.06A/B/C/D/E/F2-201[»]
    3PCFX-ray2.15A/B/C/D/E/F2-201[»]
    3PCGX-ray1.96A/B/C/D/E/F2-201[»]
    3PCHX-ray2.05A/B/C/D/E/F2-201[»]
    3PCIX-ray2.21A/B/C/D/E/F2-201[»]
    3PCJX-ray2.13A/B/C/D/E/F2-201[»]
    3PCKX-ray2.13A/B/C/D/E/F2-201[»]
    3PCLX-ray2.15A/B/C/D/E/F2-201[»]
    3PCMX-ray2.25A/B/C/D/E/F2-201[»]
    3PCNX-ray2.40A/B/C/D/E/F2-201[»]
    3T63X-ray1.54A/B/C2-201[»]
    3T67X-ray1.67A/B/C2-201[»]
    ProteinModelPortaliP00436.
    SMRiP00436. Positions 2-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00436.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di2.60.130.10. 1 hit.
    InterProiIPR000627. Intradiol_dOase_C.
    IPR015889. Intradiol_dOase_core.
    IPR012786. Protocat_dOase_a.
    [Graphical view]
    PfamiPF00775. Dioxygenase_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF49482. SSF49482. 1 hit.
    TIGRFAMsiTIGR02423. protocat_alph. 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.

    P00436-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPIELLPETP SQTAGPYVHI GLALEAAGNP TRDQEIWNRL AKPDAPGEHI    50
    LLLGQVYDGN GHLVRDSFLE VWQADANGEY QDAYNLENAF NSFGRTATTF 100
    DAGEWTLHTV KPGVVNNAAG VPMAPHINIS LFARGINIHL HTRLYFDDEA 150
    QANAKCPVLN LIEQPQRRET LIAKRCEVDG KTAYRFDIRI QGEGETVFFD 200
    F 201
    Length:201
    Mass (Da):22,387
    Last modified:January 23, 2007 - v3
    Checksum:iBF95DB892076FBAF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601N → D AA sequence (PubMed:465136)Curated
    Sequence conflicti77 – 771N → D AA sequence (PubMed:465136)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14836 Genomic DNA. Translation: AAB41025.1.
    PIRiB36930. DAPSAA.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14836 Genomic DNA. Translation: AAB41025.1 .
    PIRi B36930. DAPSAA.

    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 A/C/E/G/I/K 2-201 [» ]
    1YKL X-ray 2.25 A/C/E/G/I/K 2-201 [» ]
    1YKM X-ray 2.22 A/C/E/G/I/K 2-201 [» ]
    1YKN X-ray 2.06 A/C/E/G/I/K 2-201 [» ]
    1YKO X-ray 2.54 A/C/E/G/I/K 2-201 [» ]
    1YKP X-ray 2.41 A/C/E/G/I/K 2-201 [» ]
    2PCD X-ray 2.15 A/B/C/D/E/F 2-201 [» ]
    3LKT X-ray 1.65 A/B/C/D/E/F 2-201 [» ]
    3LMX X-ray 2.20 A/B/C 2-201 [» ]
    3LXV X-ray 1.90 A/B/C 2-201 [» ]
    3MFL X-ray 1.78 A/B/C 2-201 [» ]
    3MI1 X-ray 1.74 A/B/C 2-201 [» ]
    3MI5 X-ray 1.78 A/B/C/D/E/F 2-201 [» ]
    3MV4 X-ray 1.59 A/B/C 2-201 [» ]
    3MV6 X-ray 1.86 A/B/C 2-201 [» ]
    3PCA X-ray 2.20 A/B/C/D/E/F 2-201 [» ]
    3PCB X-ray 2.19 A/B/C/D/E/F 2-201 [» ]
    3PCC X-ray 1.98 A/B/C/D/E/F 2-201 [» ]
    3PCD X-ray 2.10 A/B/C/D/E/F 2-201 [» ]
    3PCE X-ray 2.06 A/B/C/D/E/F 2-201 [» ]
    3PCF X-ray 2.15 A/B/C/D/E/F 2-201 [» ]
    3PCG X-ray 1.96 A/B/C/D/E/F 2-201 [» ]
    3PCH X-ray 2.05 A/B/C/D/E/F 2-201 [» ]
    3PCI X-ray 2.21 A/B/C/D/E/F 2-201 [» ]
    3PCJ X-ray 2.13 A/B/C/D/E/F 2-201 [» ]
    3PCK X-ray 2.13 A/B/C/D/E/F 2-201 [» ]
    3PCL X-ray 2.15 A/B/C/D/E/F 2-201 [» ]
    3PCM X-ray 2.25 A/B/C/D/E/F 2-201 [» ]
    3PCN X-ray 2.40 A/B/C/D/E/F 2-201 [» ]
    3T63 X-ray 1.54 A/B/C 2-201 [» ]
    3T67 X-ray 1.67 A/B/C 2-201 [» ]
    ProteinModelPortali P00436.
    SMRi P00436. Positions 2-201.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00436. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00157 ; UER00264 .
    BioCyci MetaCyc:MONOMER-3186.
    RETL1328306-WGS:GSTH-5904-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P00436.

    Family and domain databases

    Gene3Di 2.60.130.10. 1 hit.
    InterProi IPR000627. Intradiol_dOase_C.
    IPR015889. Intradiol_dOase_core.
    IPR012786. Protocat_dOase_a.
    [Graphical view ]
    Pfami PF00775. Dioxygenase_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49482. SSF49482. 1 hit.
    TIGRFAMsi TIGR02423. protocat_alph. 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 primary structure of the alpha subunit of protocatechuate 3,4-dioxygenase. II. Isolation and sequence of overlap peptides and complete sequence."
      Kohlmiller N.A., Howard J.B.
      J. Biol. Chem. 254:7309-7315(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-201.
      Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
    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 nameiPCXA_PSEPU
    AccessioniPrimary (citable) accession number: P00436
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 99 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